HDA19_ARATH
ID HDA19_ARATH Reviewed; 501 AA.
AC O22446; Q0WWG3; Q9SZL3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Histone deacetylase 19 {ECO:0000303|PubMed:12466527};
DE Short=AtHD1 {ECO:0000303|PubMed:11134508};
DE Short=HD;
DE EC=3.5.1.98 {ECO:0000269|PubMed:16699543};
GN Name=HDA19 {ECO:0000303|PubMed:12466527};
GN Synonyms=HD1 {ECO:0000303|PubMed:11134508}, HDA1,
GN RPD3A {ECO:0000303|PubMed:11117260};
GN OrderedLocusNames=At4g38130 {ECO:0000312|Araport:AT4G38130};
GN ORFNames=F20D10.250 {ECO:0000312|EMBL:CAB37553.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Tomihama T., Shoji K., Hanyu H., Okano T.;
RT "Characterization of a histone deacetylase (EST G11C3T7) in Arabidopsis
RT thaliana.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=11117260; DOI=10.1023/a:1006498413543;
RA Wu K., Malik K., Tian L., Brown D., Miki B.;
RT "Functional analysis of a RPD3 histone deacetylase homologue in Arabidopsis
RT thaliana.";
RL Plant Mol. Biol. 44:167-176(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11134508; DOI=10.1073/pnas.98.1.200;
RA Tian L., Chen Z.J.;
RT "Blocking histone deacetylation in Arabidopsis induces pleiotropic effects
RT on plant gene regulation and development.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:200-205(2001).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12466527; DOI=10.1093/nar/gkf660;
RA Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S.,
RA Richards E.J., Bender J., Mount D.W., Jorgensen R.A.;
RT "Analysis of histone acetyltransferase and histone deacetylase families of
RT Arabidopsis thaliana suggests functional diversification of chromatin
RT modification among multicellular eukaryotes.";
RL Nucleic Acids Res. 30:5036-5055(2002).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=15749761; DOI=10.1105/tpc.104.028514;
RA Zhou C., Zhang L., Duan J., Miki B., Wu K.;
RT "HISTONE DEACETYLASE19 is involved in jasmonic acid and ethylene signaling
RT of pathogen response in Arabidopsis.";
RL Plant Cell 17:1196-1204(2005).
RN [10]
RP INTERACTION WITH SIN3.
RX PubMed=15994908; DOI=10.1105/tpc.105.033043;
RA Song C.-P., Agarwal M., Ohta M., Guo Y., Halfter U., Wang P., Zhu J.-K.;
RT "Role of an Arabidopsis AP2/EREBP-type transcriptional repressor in
RT abscisic acid and drought stress responses.";
RL Plant Cell 17:2384-2396(2005).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=16699543; DOI=10.1038/sj.cr.7310059;
RA Fong P.M., Tian L., Chen Z.J.;
RT "Arabidopsis thaliana histone deacetylase 1 (AtHD1) is localized in
RT euchromatic regions and demonstrates histone deacetylase activity in
RT vitro.";
RL Cell Res. 16:479-488(2006).
RN [12]
RP INTERACTION WITH SAP18.
RX PubMed=16429262; DOI=10.1007/s11103-005-3880-9;
RA Song C.-P., Galbraith D.W.;
RT "AtSAP18, an orthologue of human SAP18, is involved in the regulation of
RT salt stress and mediates transcriptional repression in Arabidopsis.";
RL Plant Mol. Biol. 60:241-257(2006).
RN [13]
RP INTERACTION WITH MED14; LUG AND CDKE-1.
RX PubMed=17526732; DOI=10.1128/mcb.01912-06;
RA Gonzalez D., Bowen A.J., Carroll T.S., Conlan R.S.;
RT "The transcription corepressor LEUNIG interacts with the histone
RT deacetylase HDA19 and mediator components MED14 (SWP) and CDK8 (HEN3) to
RT repress transcription.";
RL Mol. Cell. Biol. 27:5306-5315(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [15]
RP INTERACTION WITH TPR1.
RX PubMed=20647385; DOI=10.1073/pnas.1002828107;
RA Zhu Z., Xu F., Zhang Y., Cheng Y.T., Wiermer M., Li X., Zhang Y.;
RT "Arabidopsis resistance protein SNC1 activates immune responses through
RT association with a transcriptional corepressor.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13960-13965(2010).
RN [16]
RP FUNCTION, AND INTERACTION WITH TPL.
RX PubMed=23034631; DOI=10.1242/dev.085407;
RA Krogan N.T., Hogan K., Long J.A.;
RT "APETALA2 negatively regulates multiple floral organ identity genes in
RT Arabidopsis by recruiting the co-repressor TOPLESS and the histone
RT deacetylase HDA19.";
RL Development 139:4180-4190(2012).
RN [17]
RP INTERACTION WITH AHL22.
RX PubMed=22442143; DOI=10.1074/jbc.m111.318477;
RA Yun J., Kim Y.S., Jung J.H., Seo P.J., Park C.M.;
RT "The AT-hook motif-containing protein AHL22 regulates flowering initiation
RT by modifying FLOWERING LOCUS T chromatin in Arabidopsis.";
RL J. Biol. Chem. 287:15307-15316(2012).
RN [18]
RP FUNCTION.
RX PubMed=29018096; DOI=10.1104/pp.17.01332;
RA Ueda M., Matsui A., Tanaka M., Nakamura T., Abe T., Sako K., Sasaki T.,
RA Kim J.M., Ito A., Nishino N., Shimada H., Yoshida M., Seki M.;
RT "The distinct roles of class I and II RPD3-like histone deacetylases in
RT salinity stress response.";
RL Plant Physiol. 175:1760-1773(2017).
CC -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC deacetylation gives a tag for epigenetic repression and plays an
CC important role in transcriptional regulation, cell cycle progression
CC and developmental events. Histone deacetylases act via the formation of
CC large multiprotein complexes. HDA19 is involved in jasmonic acid and
CC ethylene signaling of pathogen response. Part of a repressor complex
CC including APETALA2 (AP2) and TOPLESS (TPL) that control the expression
CC domains of numerous floral organ identity genes (PubMed:23034631).
CC Involved in negative regulation of salinity stress response
CC (PubMed:29018096). Represses the expression of stress tolerance-related
CC genes, genes coding for late embryogenesis abundant (LEA) proteins that
CC prevent protein aggregation, and positive regulators of abscisic acid
CC (ABA) signaling, such as ABI5 and NAC019 (PubMed:29018096).
CC {ECO:0000269|PubMed:11117260, ECO:0000269|PubMed:11134508,
CC ECO:0000269|PubMed:15749761, ECO:0000269|PubMed:16699543,
CC ECO:0000269|PubMed:23034631, ECO:0000269|PubMed:29018096}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; EC=3.5.1.98;
CC Evidence={ECO:0000269|PubMed:16699543};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q8GXJ1};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q8GXJ1};
CC -!- SUBUNIT: Interacts with SIN3, SAP18 and TPR1. Interacts with CDKE-1,
CC MED14 and LUG. Interacts with TPL (PubMed:23034631). Interacts with
CC AHL22 (PubMed:22442143). {ECO:0000269|PubMed:15994908,
CC ECO:0000269|PubMed:16429262, ECO:0000269|PubMed:17526732,
CC ECO:0000269|PubMed:20647385, ECO:0000269|PubMed:22442143,
CC ECO:0000269|PubMed:23034631}.
CC -!- INTERACTION:
CC O22446; O64644: At2g45640; NbExp=2; IntAct=EBI-593040, EBI-965964;
CC O22446; Q8GWF1: WRKY38; NbExp=2; IntAct=EBI-593040, EBI-1993263;
CC O22446; Q9LZV6: WRKY62; NbExp=5; IntAct=EBI-593040, EBI-1993243;
CC O22446; Q6DLS1: SCL1; Xeno; NbExp=3; IntAct=EBI-593040, EBI-593035;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15749761,
CC ECO:0000269|PubMed:16699543}. Note=excluded from the nucleolus, but
CC associated with the condensing chromatids.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O22446-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves, stems, flowers and
CC young siliques. {ECO:0000269|PubMed:11117260,
CC ECO:0000269|PubMed:11134508, ECO:0000269|PubMed:16699543}.
CC -!- INDUCTION: Induced by jasmonic acid, ethylene, wounding and pathogen
CC infection. Inhibited by sodium butyrate. {ECO:0000269|PubMed:15749761,
CC ECO:0000269|PubMed:16699543}.
CC -!- MISCELLANEOUS: Loss-of-function mutant (antisense inhibition) has an
CC increased level of tetraacetylated histone H4 and shows late flowering,
CC developmental pleiotropy and increased symptoms when infected by a
CC pathogen. {ECO:0000269|PubMed:11134508}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; AF014824; AAB66486.1; -; mRNA.
DR EMBL; AF195547; AAG28474.1; -; mRNA.
DR EMBL; AL035538; CAB37553.1; -; Genomic_DNA.
DR EMBL; AL161593; CAB80478.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86881.1; -; Genomic_DNA.
DR EMBL; AY093153; AAM13152.1; -; mRNA.
DR EMBL; BT008873; AAP68312.1; -; mRNA.
DR EMBL; AK226389; BAE98535.1; -; mRNA.
DR PIR; T05640; T05640.
DR RefSeq; NP_195526.1; NM_119974.4. [O22446-1]
DR AlphaFoldDB; O22446; -.
DR SMR; O22446; -.
DR BioGRID; 15249; 18.
DR DIP; DIP-33483N; -.
DR IntAct; O22446; 8.
DR STRING; 3702.AT4G38130.1; -.
DR iPTMnet; O22446; -.
DR PaxDb; O22446; -.
DR PRIDE; O22446; -.
DR ProteomicsDB; 230288; -. [O22446-1]
DR EnsemblPlants; AT4G38130.1; AT4G38130.1; AT4G38130. [O22446-1]
DR GeneID; 829969; -.
DR Gramene; AT4G38130.1; AT4G38130.1; AT4G38130. [O22446-1]
DR KEGG; ath:AT4G38130; -.
DR Araport; AT4G38130; -.
DR TAIR; locus:2120948; AT4G38130.
DR eggNOG; KOG1342; Eukaryota.
DR InParanoid; O22446; -.
DR PhylomeDB; O22446; -.
DR BRENDA; 3.5.1.98; 399.
DR PRO; PR:O22446; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O22446; baseline and differential.
DR Genevisible; O22446; AT.
DR GO; GO:0000118; C:histone deacetylase complex; IPI:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0016580; C:Sin3 complex; IDA:TAIR.
DR GO; GO:0004407; F:histone deacetylase activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0009294; P:DNA-mediated transformation; IMP:TAIR.
DR GO; GO:0016573; P:histone acetylation; IDA:TAIR.
DR GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR GO; GO:0009861; P:jasmonic acid and ethylene-dependent systemic resistance; IMP:TAIR.
DR GO; GO:1901001; P:negative regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IGI:TAIR.
DR GO; GO:2000026; P:regulation of multicellular organismal development; IMP:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.40.800.20; -; 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR003084; His_deacetylse_1.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR PRINTS; PR01270; HDASUPER.
DR PRINTS; PR01271; HISDACETLASE.
DR SUPFAM; SSF52768; SSF52768; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Hydrolase; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..501
FT /note="Histone deacetylase 19"
FT /id="PRO_0000114721"
FT REGION 17..329
FT /note="Histone deacetylase"
FT REGION 383..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT SITE 311
FT /note="Polarizes the scissile carbonyl of the substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 69
FT /note="D -> E (in Ref. 1; AAB66486 and 2; AAG28474)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 56023 MW; 857D2E3D16B7CC1F CRC64;
MDTGGNSLAS GPDGVKRKVC YFYDPEVGNY YYGQGHPMKP HRIRMTHALL AHYGLLQHMQ
VLKPFPARDR DLCRFHADDY VSFLRSITPE TQQDQIRQLK RFNVGEDCPV FDGLYSFCQT
YAGGSVGGSV KLNHGLCDIA INWAGGLHHA KKCEASGFCY VNDIVLAILE LLKQHERVLY
VDIDIHHGDG VEEAFYATDR VMTVSFHKFG DYFPGTGHIQ DIGYGSGKYY SLNVPLDDGI
DDESYHLLFK PIMGKVMEIF RPGAVVLQCG ADSLSGDRLG CFNLSIKGHA ECVKFMRSFN
VPLLLLGGGG YTIRNVARCW CYETGVALGV EVEDKMPEHE YYEYFGPDYT LHVAPSNMEN
KNSRQMLEEI RNDLLHNLSK LQHAPSVPFQ ERPPDTETPE VDEDQEDGDK RWDPDSDMDV
DDDRKPIPSR VKREAVEPDT KDKDGLKGIM ERGKGCEVEV DESGSTKVTG VNPVGVEEAS
VKMEEEGTNK GGAEQAFPPK T
