NUD19_HUMAN
ID NUD19_HUMAN Reviewed; 375 AA.
AC A8MXV4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Acyl-coenzyme A diphosphatase NUDT19;
DE EC=3.6.1.-;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 19;
DE Short=Nudix motif 19;
GN Name=NUDT19;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes
CC fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-
CC bisphosphate (By similarity). Mediates the hydrolysis of a wide range
CC of CoA esters, including choloyl-CoA and branched-chain fatty-acyl-CoA
CC esters and at low substrate concentrations medium and long-chain fatty-
CC acyl-CoA esters are the primary substrates (By similarity). Highest
CC activity seen with medium-chain acyl-CoA esters and higher rates of
CC activity seen with the unsaturated acyl-CoA esters compared with the
CC saturated esters (By similarity). Exhibits decapping activity towards
CC dpCoA-capped RNAs in vitro (By similarity).
CC {ECO:0000250|UniProtKB:P11930}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + H2O = adenosine 3',5'-bisphosphate + an acyl-4'-
CC phosphopantetheine + 2 H(+); Xref=Rhea:RHEA:50044, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58342, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:132023; Evidence={ECO:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50045;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CoA + H2O = (R)-4'-phosphopantetheine + adenosine 3',5'-
CC bisphosphate + 2 H(+); Xref=Rhea:RHEA:64988, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:61723; Evidence={ECO:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64989;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) +
CC hexanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:49980,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:62620, ChEBI:CHEBI:132012;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49981;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) +
CC S-octanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50016,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132013;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50017;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) +
CC S-butanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:49976,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57371,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132011;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49977;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + propanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) +
CC propanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:67464,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:172362;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67465;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + malonyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) +
CC malonyl-4'-phosphopantetheine; Xref=Rhea:RHEA:67468,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:172363;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67469;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + succinyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) +
CC succinyl-4'-phosphopantetheine; Xref=Rhea:RHEA:67472,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:172364;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67473;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choloyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + S-
CC choloyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50036,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57373,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132020;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50037;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4,8-dimethylnonanoyl-CoA + H2O = adenosine 3',5'-bisphosphate
CC + 2 H(+) + S-(4,8-dimethylnonanoyl)-4'-phosphopantetheine;
CC Xref=Rhea:RHEA:67524, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:77061, ChEBI:CHEBI:172385;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67525;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + H2O = adenosine 3',5'-
CC bisphosphate + 2 H(+) + S-(9Z,12Z,15Z-octadecatrienoyl)-4'-
CC phosphopantetheine; Xref=Rhea:RHEA:67532, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58343, ChEBI:CHEBI:74034,
CC ChEBI:CHEBI:172386; Evidence={ECO:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67533;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + H2O = adenosine 3',5'-
CC bisphosphate + 2 H(+) + S-(9Z,12Z-octadecadienoyl)-4'-
CC phosphopantetheine; Xref=Rhea:RHEA:67536, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57383, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:172387; Evidence={ECO:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67537;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2
CC H(+) + S-(9Z-hexadecenoyl)-4'-phosphopantetheine;
CC Xref=Rhea:RHEA:67540, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:61540, ChEBI:CHEBI:172388;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67541;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-tetradecenoyl-CoA + H2O = adenosine 3',5'-bisphosphate +
CC 2 H(+) + S-(9Z-tetradecenoyl)-4'-phosphopantetheine;
CC Xref=Rhea:RHEA:67544, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:65060, ChEBI:CHEBI:172389;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67545;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6Z)-octenoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2
CC H(+) + S-(6Z-octenoyl)-4'-phosphopantetheine; Xref=Rhea:RHEA:67528,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:172383, ChEBI:CHEBI:172384;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67529;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+)
CC + S-hexadecanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50032,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132018;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50033;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetradecanoyl-CoA = adenosine 3',5'-bisphosphate + 2
CC H(+) + tetradecanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50028,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132017;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50029;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) +
CC S-dodecanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50024,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132015;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50025;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end CoA-ribonucleoside in mRNA + H2O = (R)-4'-
CC phosphopantetheine + a 5'-end phospho-adenosine-phospho-
CC ribonucleoside in mRNA + 2 H(+); Xref=Rhea:RHEA:67592, Rhea:RHEA-
CC COMP:15719, Rhea:RHEA-COMP:17276, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:61723, ChEBI:CHEBI:144051,
CC ChEBI:CHEBI:172371; Evidence={ECO:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67593;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P11930}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:P11930}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AC008736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS42543.1; -.
DR RefSeq; NP_001099040.1; NM_001105570.1.
DR AlphaFoldDB; A8MXV4; -.
DR BioGRID; 133735; 117.
DR IntAct; A8MXV4; 26.
DR MINT; A8MXV4; -.
DR STRING; 9606.ENSP00000380251; -.
DR iPTMnet; A8MXV4; -.
DR PhosphoSitePlus; A8MXV4; -.
DR BioMuta; NUDT19; -.
DR EPD; A8MXV4; -.
DR jPOST; A8MXV4; -.
DR MassIVE; A8MXV4; -.
DR MaxQB; A8MXV4; -.
DR PaxDb; A8MXV4; -.
DR PeptideAtlas; A8MXV4; -.
DR PRIDE; A8MXV4; -.
DR ProteomicsDB; 2356; -.
DR Antibodypedia; 44300; 99 antibodies from 19 providers.
DR DNASU; 390916; -.
DR Ensembl; ENST00000397061.4; ENSP00000380251.2; ENSG00000213965.4.
DR GeneID; 390916; -.
DR KEGG; hsa:390916; -.
DR MANE-Select; ENST00000397061.4; ENSP00000380251.2; NM_001105570.2; NP_001099040.1.
DR UCSC; uc010edf.3; human.
DR CTD; 390916; -.
DR DisGeNET; 390916; -.
DR GeneCards; NUDT19; -.
DR HGNC; HGNC:32036; NUDT19.
DR HPA; ENSG00000213965; Low tissue specificity.
DR neXtProt; NX_A8MXV4; -.
DR OpenTargets; ENSG00000213965; -.
DR PharmGKB; PA142671239; -.
DR VEuPathDB; HostDB:ENSG00000213965; -.
DR eggNOG; KOG3904; Eukaryota.
DR GeneTree; ENSGT00420000029858; -.
DR HOGENOM; CLU_059078_1_0_1; -.
DR InParanoid; A8MXV4; -.
DR OMA; SPHQGFM; -.
DR OrthoDB; 1417901at2759; -.
DR PhylomeDB; A8MXV4; -.
DR TreeFam; TF313185; -.
DR PathwayCommons; A8MXV4; -.
DR Reactome; R-HSA-390918; Peroxisomal lipid metabolism.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SignaLink; A8MXV4; -.
DR BioGRID-ORCS; 390916; 5 hits in 1080 CRISPR screens.
DR ChiTaRS; NUDT19; human.
DR GenomeRNAi; 390916; -.
DR Pharos; A8MXV4; Tdark.
DR PRO; PR:A8MXV4; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; A8MXV4; protein.
DR Bgee; ENSG00000213965; Expressed in vastus lateralis and 185 other tissues.
DR Genevisible; A8MXV4; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0106399; F:acyl-coenzyme A diphosphatase activity; IEA:RHEA.
DR GO; GO:0010945; F:CoA pyrophosphatase activity; TAS:Reactome.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0044580; P:butyryl-CoA catabolic process; ISS:UniProtKB.
DR GO; GO:0015938; P:coenzyme A catabolic process; ISS:UniProtKB.
DR GO; GO:0009062; P:fatty acid catabolic process; TAS:Reactome.
DR GO; GO:2001294; P:malonyl-CoA catabolic process; ISS:UniProtKB.
DR GO; GO:0036114; P:medium-chain fatty-acyl-CoA catabolic process; ISS:UniProtKB.
DR GO; GO:1902858; P:propionyl-CoA metabolic process; ISS:UniProtKB.
DR GO; GO:1901289; P:succinyl-CoA catabolic process; ISS:UniProtKB.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR039121; NUDT19.
DR PANTHER; PTHR12318; PTHR12318; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Peroxisome;
KW Reference proteome.
FT CHAIN 1..375
FT /note="Acyl-coenzyme A diphosphatase NUDT19"
FT /id="PRO_0000324571"
FT DOMAIN 15..263
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 91..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 116..137
FT /note="Nudix box"
FT MOTIF 373..375
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11930"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11930"
FT SITE 49
FT /note="Important for coenzyme A binding"
FT /evidence="ECO:0000250|UniProtKB:P11930"
FT SITE 55
FT /note="Important for coenzyme A binding"
FT /evidence="ECO:0000250|UniProtKB:P11930"
FT SITE 210
FT /note="Important for coenzyme A binding"
FT /evidence="ECO:0000250|UniProtKB:P11930"
FT VARIANT 43
FT /note="R -> Q (in dbSNP:rs10413282)"
FT /id="VAR_039831"
SQ SEQUENCE 375 AA; 42233 MW; D02AE72BE8615DA3 CRC64;
MSSSLRPGPS RWRRAASIVL AAGWSRPETA TPPSRPPPAE GFRLLLLQRS PHQGFMPGAH
VFSGGVLDAA DRSADWLGLF APHHGPPRFG LGPAPFSRTA FPSLPDTDDH KTDNTGTLPE
DVAFRICAVR EAFEEAGVLL LRPRTSPPGP APGPGLALEP PPGLASWRDR VRQDPRHFLR
LCAHLDCTPD IWALHNWSAW LTPFLRGTTR RFDTAFFLCC LREPPPVYPD LAEVVGYQWS
SPSEATESFL SKEIWLPPPQ FYEVRRLANF ASLSDLHKFC LGRALEGLER WLPIILLTAD
GMVHLLPGDE LYLEDSDFLE NLMSTEKKTE EIMKEGKQFH RIVTYHRHLY DIHVTVQPKY
KHVYPKNSVV RKSHL
