MOCOS_ARATH
ID MOCOS_ARATH Reviewed; 819 AA.
AC Q9C5X8; Q9FX72;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Molybdenum cofactor sulfurase {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MCS {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MOS {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MoCo sulfurase {ECO:0000255|HAMAP-Rule:MF_03050};
DE EC=2.8.1.9 {ECO:0000255|HAMAP-Rule:MF_03050, ECO:0000269|PubMed:11553608, ECO:0000269|PubMed:15561708};
DE AltName: Full=Abscisic acid protein 3;
DE AltName: Full=Low expression of osmotically expressive genes protein 5;
DE AltName: Full=Molybdenum cofactor sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03050};
GN Name=ABA3; Synonyms=LOS5; OrderedLocusNames=At1g16540; ORFNames=F19K19.13;
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], FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS
RP OF GLY-469.
RX PubMed=11553608; DOI=10.1074/jbc.c100472200;
RA Bittner F., Oreb M., Mendel R.R.;
RT "ABA3 is a molybdenum cofactor sulfurase required for activation of
RT aldehyde oxidase and xanthine dehydrogenase in Arabidopsis thaliana.";
RL J. Biol. Chem. 276:40381-40384(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND
RP MUTAGENESIS OF GLY-106 AND GLY-469.
RX PubMed=11549764; DOI=10.2307/3871428;
RA Xiong L., Ishitani M., Lee H., Zhu J.-K.;
RT "The arabidopsis los5/aba3 locus encodes a molybdenum cofactor sulfurase
RT and modulates cold stress- and osmotic stress-responsive gene expression.";
RL Plant Cell 13:2063-2083(2001).
RN [3]
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 [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 FUNCTION.
RX PubMed=14726515; DOI=10.1074/jbc.m312929200;
RA Hesberg C., Haensch R., Mendel R.R., Bittner F.;
RT "Tandem orientation of duplicated xanthine dehydrogenase genes from
RT Arabidopsis thaliana: differential gene expression and enzyme activities.";
RL J. Biol. Chem. 279:13547-13554(2004).
RN [6]
RP COFACTOR, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP PYRIDOXAL PHOSPHATE AT LYS-271, AND MUTAGENESIS OF LYS-271 AND CYS-430.
RX PubMed=15561708; DOI=10.1074/jbc.m411195200;
RA Heidenreich T., Wollers S., Mendel R.R., Bittner F.;
RT "Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana
RT provides insight into the mechanism of molybdenum cofactor sulfuration.";
RL J. Biol. Chem. 280:4213-4218(2005).
RN [7]
RP FUNCTION OF C-TERMINAL DOMAIN.
RX PubMed=18258600; DOI=10.1074/jbc.m708549200;
RA Wollers S., Heidenreich T., Zarepour M., Zachmann D., Kraft C., Zhao Y.,
RA Mendel R.R., Bittner F.;
RT "Binding of sulfurated molybdenum cofactor to the C-terminal domain of ABA3
RT from Arabidopsis thaliana provides insight into the mechanism of molybdenum
RT cofactor sulfuration.";
RL J. Biol. Chem. 283:9642-9650(2008).
CC -!- FUNCTION: Sulfurates the molybdenum cofactor. Sulfation of molybdenum
CC is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase
CC (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and
CC 1 sulfur atom in active form. Modulates cold stress- and osmotic
CC stress-responsive gene expression by acting as key regulator of
CC abscisic acid (ABA) biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03050,
CC ECO:0000269|PubMed:11549764, ECO:0000269|PubMed:11553608,
CC ECO:0000269|PubMed:14726515, ECO:0000269|PubMed:15561708,
CC ECO:0000269|PubMed:18258600}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine +
CC thio-Mo-molybdopterin; Xref=Rhea:RHEA:42636, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:71302, ChEBI:CHEBI:82685; EC=2.8.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03050,
CC ECO:0000269|PubMed:11553608, ECO:0000269|PubMed:15561708};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03050,
CC ECO:0000269|PubMed:15561708};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for L-cysteine {ECO:0000269|PubMed:15561708};
CC KM=200 uM for L-selenocysteine {ECO:0000269|PubMed:15561708};
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:11549764}.
CC -!- INDUCTION: Up-regulated in response to drought, salt or ABA treatment.
CC {ECO:0000269|PubMed:11549764}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. MOCOS subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03050}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG10824.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF325457; AAK12939.1; -; mRNA.
DR EMBL; AY034895; AAK58888.1; -; mRNA.
DR EMBL; AC011808; AAG10824.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29467.1; -; Genomic_DNA.
DR PIR; G86300; G86300.
DR RefSeq; NP_564001.1; NM_101519.3.
DR AlphaFoldDB; Q9C5X8; -.
DR SMR; Q9C5X8; -.
DR STRING; 3702.AT1G16540.1; -.
DR iPTMnet; Q9C5X8; -.
DR PaxDb; Q9C5X8; -.
DR PRIDE; Q9C5X8; -.
DR ProteomicsDB; 238297; -.
DR EnsemblPlants; AT1G16540.1; AT1G16540.1; AT1G16540.
DR GeneID; 838224; -.
DR Gramene; AT1G16540.1; AT1G16540.1; AT1G16540.
DR KEGG; ath:AT1G16540; -.
DR Araport; AT1G16540; -.
DR TAIR; locus:2017943; AT1G16540.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_1_1; -.
DR InParanoid; Q9C5X8; -.
DR PhylomeDB; Q9C5X8; -.
DR BRENDA; 2.8.1.9; 399.
DR SABIO-RK; Q9C5X8; -.
DR PRO; PR:Q9C5X8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C5X8; baseline and differential.
DR Genevisible; Q9C5X8; AT.
DR GO; GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; IDA:TAIR.
DR GO; GO:0102867; F:molybdenum cofactor sulfurtransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009000; F:selenocysteine lyase activity; IDA:TAIR.
DR GO; GO:0009688; P:abscisic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0018315; P:molybdenum incorporation into molybdenum-molybdopterin complex; IDA:TAIR.
DR GO; GO:0045037; P:protein import into chloroplast stroma; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0009749; P:response to glucose; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0010118; P:stomatal movement; IMP:TAIR.
DR GO; GO:0010182; P:sugar mediated signaling pathway; TAS:TAIR.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_03050; MOCOS; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR005302; MoCF_Sase_C.
DR InterPro; IPR028886; MoCo_sulfurase.
DR InterPro; IPR005303; MOSC_N.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR Pfam; PF00266; Aminotran_5; 2.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03476; MOSC_N; 1.
DR SUPFAM; SSF50800; SSF50800; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 1: Evidence at protein level;
KW Molybdenum cofactor biosynthesis; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..819
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000249958"
FT DOMAIN 650..817
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT ACT_SITE 430
FT MOD_RES 271
FT /note="N6-(pyridoxal phosphate)lysine"
FT MUTAGEN 106
FT /note="G->E: In los5-1; induces a deficiency in stress-
FT induced ABA accumulation."
FT /evidence="ECO:0000269|PubMed:11549764"
FT MUTAGEN 271
FT /note="K->S: Loss of function."
FT /evidence="ECO:0000269|PubMed:15561708"
FT MUTAGEN 430
FT /note="C->A: Induces a strong reduction in enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:15561708"
FT MUTAGEN 469
FT /note="G->E: In aba3-1; induces a reduced ABA
FT biosynthesis."
FT /evidence="ECO:0000269|PubMed:11549764,
FT ECO:0000269|PubMed:11553608"
SQ SEQUENCE 819 AA; 91803 MW; 81FE806B186B4007 CRC64;
MEAFLKEFGD YYGYPDGPKN IQEIRDTEFK RLDKGVVYLD HAGSTLYSEL QMEYIFKDFT
SNVFGNPHSQ SDISSATSDL IADARHQVLE YFNASPEDYS CLFTSGATAA LKLVGETFPW
TQDSNFLYTM ENHNSVLGIR EYALAQGASA CAVDIEEAAN QPGQLTNSGP SIKVKHRAVQ
MRNTSKLQKE ESRGNAYNLF AFPSECNFSG LRFNLDLVKL MKENTETVLQ GSPFSKSKRW
MVLIDAAKGC ATLPPDLSEY PADFVVLSFY KLFGYPTGLG ALLVRNDAAK LLKKTYFSGG
TVAASIADID FVKRRERVEE FFEDGSASFL SIAAIRHGFK LLKSLTPSAI WMHTTSLSIY
VKKKLQALRH GNGAAVCVLY GSENLELSSH KSGPTVTFNL KRPDGSWFGY LEVEKLASLS
GIQLRTGCFC NPGACAKYLE LSHSELRSNV EAGHICWDDN DVINGKPTGA VRVSFGYMST
FEDAKKFIDF IISSFASPPK KTGNGTVVSG RFPQLPSEDL ESKESFPSHY LKSITVYPIK
SCAGFSVIRW PLCRTGLLHD REWMVQGLTG EILTQKKVPE MSLIKTFIDL EEGLLSVESS
RCEDKLHIRI KSDSYNPRND EFDSHANILE NRNEETRINR WFTNAIGRQC KLLRYSSSTS
KDCLNRNKSP GLCRDLESNI NFANEAQFLL ISEESVADLN RRLEAKDEDY KRAHEKLNPH
RFRPNLVISG GEPYGEDKWK TVKIGDNHFT SLGGCNRCQM INISNEAGLV KKSNEPLTTL
ASYRRVKGKI LFGTLLRYEI DEKRQCWIGV GEEVNPDIE
