HAL3B_ARATH
ID HAL3B_ARATH Reviewed; 201 AA.
AC P94063; Q9LP62;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable phosphopantothenoylcysteine decarboxylase;
DE EC=4.1.1.36;
DE AltName: Full=AtCoaC2;
DE AltName: Full=Halotolerance protein Hal3b;
DE Short=AtHal3b;
GN Name=HAL3B; Synonyms=COAC2; OrderedLocusNames=At1g48605;
GN ORFNames=T1N15.24, T1N15.28, T1N15_21;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10652125; DOI=10.1046/j.1365-313x.1999.00626.x;
RA Espinosa-Ruiz A., Belles J.M., Serrano R., Culianez-Macia F.A.;
RT "Arabidopsis thaliana AtHAL3: a flavoprotein related to salt and osmotic
RT tolerance and plant growth.";
RL Plant J. 20:529-539(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16415216; DOI=10.1104/pp.105.072066;
RA Rubio S., Larson T.R., Gonzalez-Guzman M., Alejandro S., Graham I.A.,
RA Serrano R., Rodriguez P.L.;
RT "An Arabidopsis mutant impaired in coenzyme A biosynthesis is sugar
RT dependent for seedling establishment.";
RL Plant Physiol. 140:830-843(2006).
CC -!- FUNCTION: Involved in plant growth and salt and osmotic tolerance.
CC Catalyzes the decarboxylation of 4'-phosphopantothenoylcysteine to 4'-
CC phosphopantetheine, a key step in coenzyme A biosynthesis. The enzyme
CC is also able to decarboxylate pantothenoylcysteine to
CC pantothenoylcysteamine. {ECO:0000269|PubMed:16415216}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine = (R)-4'-
CC phosphopantetheine + CO2; Xref=Rhea:RHEA:16793, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:59458, ChEBI:CHEBI:61723; EC=4.1.1.36;
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC Note=Binds 1 FMN per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 3/5.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, leaves, flowers,
CC developing siliques and seeds. {ECO:0000269|PubMed:10652125}.
CC -!- INDUCTION: By salt stress. {ECO:0000269|PubMed:10652125}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but homozygous double mutants hal3a-1 and hal3b are
CC embryonic lethal. {ECO:0000269|PubMed:16415216}.
CC -!- SIMILARITY: Belongs to the HFCD (homooligomeric flavin containing Cys
CC decarboxylase) superfamily. {ECO:0000305}.
CC -!- CAUTION: Was previously called At1g48610. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79709.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g48610 has been split into 2 genes: At1g48605 and At1g48610.; Evidence={ECO:0000305};
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DR EMBL; U80192; AAB53106.1; -; Genomic_DNA.
DR EMBL; AC020889; AAF79709.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32325.1; -; Genomic_DNA.
DR RefSeq; NP_973994.1; NM_202265.3.
DR AlphaFoldDB; P94063; -.
DR SMR; P94063; -.
DR BioGRID; 30426; 1.
DR STRING; 3702.AT1G48605.1; -.
DR PaxDb; P94063; -.
DR PRIDE; P94063; -.
DR ProteomicsDB; 230296; -.
DR EnsemblPlants; AT1G48605.1; AT1G48605.1; AT1G48605.
DR GeneID; 2745818; -.
DR Gramene; AT1G48605.1; AT1G48605.1; AT1G48605.
DR KEGG; ath:AT1G48605; -.
DR Araport; AT1G48605; -.
DR TAIR; locus:1006230763; AT1G48605.
DR eggNOG; KOG0672; Eukaryota.
DR HOGENOM; CLU_033319_3_2_1; -.
DR InParanoid; P94063; -.
DR OMA; RKWAHIL; -.
DR OrthoDB; 1225808at2759; -.
DR PhylomeDB; P94063; -.
DR BioCyc; ARA:AT1G48605-MON; -.
DR UniPathway; UPA00241; UER00354.
DR PRO; PR:P94063; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P94063; baseline and differential.
DR GO; GO:0071513; C:phosphopantothenoylcysteine decarboxylase complex; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; ISS:TAIR.
DR GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; IBA:GO_Central.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IMP:TAIR.
DR GO; GO:0042538; P:hyperosmotic salinity response; IEP:TAIR.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1950; -; 1.
DR InterPro; IPR036551; Flavin_trans-like.
DR InterPro; IPR003382; Flavoprotein.
DR Pfam; PF02441; Flavoprotein; 1.
DR SUPFAM; SSF52507; SSF52507; 1.
PE 2: Evidence at transcript level;
KW Coenzyme A biosynthesis; Decarboxylase; Flavoprotein; FMN;
KW Growth regulation; Lyase; Reference proteome; Stress response.
FT CHAIN 1..201
FT /note="Probable phosphopantothenoylcysteine decarboxylase"
FT /id="PRO_0000182033"
FT ACT_SITE 167
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 20..22
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 45..47
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 98..101
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164..166
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 201 AA; 22415 MW; 7962655E408FA64C CRC64;
MNMEVDTVTR KPRILLAASG SVASIKFSNL CHCFSEWAEV KAVASKSSLN FVDKPSLPQN
VTLYTDEDEW SSWNKIGDPV LHIELRRWAD VMIIAPLSAN TLAKIAGGLC DNLLTCIVRA
WDYSKPLFVA PAMNTLMWNN PFTERHLVLL DELGITLIPP IKKKLACGDY GNGAMAEPSL
IYSTVRLFWE SQARKQRDGT S
