MOC2B_ARATH
ID MOC2B_ARATH Reviewed; 198 AA.
AC O22827;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Molybdopterin synthase catalytic subunit {ECO:0000255|HAMAP-Rule:MF_03052};
DE EC=2.8.1.12 {ECO:0000255|HAMAP-Rule:MF_03052};
DE AltName: Full=Molybdenum cofactor synthesis protein 2 large subunit {ECO:0000255|HAMAP-Rule:MF_03052};
DE AltName: Full=Molybdenum cofactor synthesis protein 2B {ECO:0000255|HAMAP-Rule:MF_03052};
DE Short=MOCS2B {ECO:0000255|HAMAP-Rule:MF_03052};
GN Name=MOCS2 {ECO:0000255|HAMAP-Rule:MF_03052}; Synonyms=CNX6;
GN OrderedLocusNames=At2g43760; ORFNames=F18O19.13;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10940562; DOI=10.1016/s0378-1119(00)00261-4;
RA Jost R., Berkowitz O., Wirtz M., Hopkins L., Hawkesford M.J., Hell R.;
RT "Genomic and functional characterization of the oas gene family encoding O-
RT acetylserine (thiol) lyases, enzymes catalyzing the final step in cysteine
RT biosynthesis in Arabidopsis thaliana.";
RL Gene 253:237-247(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Brinkmann H., Riedel B., Schledzewski K., Mendel R.R.;
RT "The EST clone 246M14T7 (accession W43091) encodes the large subunit of the
RT molybdopterin-synthase, an enzyme involved in molybdenum cofactor
RT biosynthesis.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
CC -!- FUNCTION: Catalytic subunit of the molybdopterin synthase complex, a
CC complex that catalyzes the conversion of precursor Z into
CC molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms
CC from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene
CC group. {ECO:0000255|HAMAP-Rule:MF_03052}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal
CC Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2
CC [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly +
CC 4 H(+) + molybdopterin; Xref=Rhea:RHEA:26333, Rhea:RHEA-COMP:12160,
CC Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58698, ChEBI:CHEBI:59648, ChEBI:CHEBI:90619,
CC ChEBI:CHEBI:90778; EC=2.8.1.12; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03052};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03052}.
CC -!- SUBUNIT: Heterotetramer; composed of 2 small (MOCS2A) and 2 large
CC (MOCS2B) subunits. {ECO:0000255|HAMAP-Rule:MF_03052}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03052}.
CC -!- SIMILARITY: Belongs to the MoaE family. MOCS2B subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03052}.
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DR EMBL; AJ271728; CAB71291.1; -; Genomic_DNA.
DR EMBL; AJ133519; CAB38428.1; -; mRNA.
DR EMBL; AC002333; AAB64030.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10319.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10320.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10321.1; -; Genomic_DNA.
DR EMBL; AF361842; AAK32854.1; -; mRNA.
DR EMBL; BT001126; AAN64517.1; -; mRNA.
DR EMBL; AK317154; BAH19840.1; -; mRNA.
DR PIR; B84870; B84870.
DR RefSeq; NP_001078051.1; NM_001084582.2.
DR RefSeq; NP_001118518.1; NM_001125046.2.
DR RefSeq; NP_181904.1; NM_129938.4.
DR AlphaFoldDB; O22827; -.
DR SMR; O22827; -.
DR BioGRID; 4315; 2.
DR STRING; 3702.AT2G43760.1; -.
DR iPTMnet; O22827; -.
DR PaxDb; O22827; -.
DR PRIDE; O22827; -.
DR ProteomicsDB; 239062; -.
DR DNASU; 818979; -.
DR EnsemblPlants; AT2G43760.1; AT2G43760.1; AT2G43760.
DR EnsemblPlants; AT2G43760.2; AT2G43760.2; AT2G43760.
DR EnsemblPlants; AT2G43760.3; AT2G43760.3; AT2G43760.
DR GeneID; 818979; -.
DR Gramene; AT2G43760.1; AT2G43760.1; AT2G43760.
DR Gramene; AT2G43760.2; AT2G43760.2; AT2G43760.
DR Gramene; AT2G43760.3; AT2G43760.3; AT2G43760.
DR KEGG; ath:AT2G43760; -.
DR Araport; AT2G43760; -.
DR TAIR; locus:2043944; AT2G43760.
DR eggNOG; KOG3307; Eukaryota.
DR HOGENOM; CLU_089568_0_0_1; -.
DR InParanoid; O22827; -.
DR OMA; WPLQRVS; -.
DR OrthoDB; 1419096at2759; -.
DR PhylomeDB; O22827; -.
DR BioCyc; ARA:AT2G43760-MON; -.
DR BioCyc; MetaCyc:AT2G43760-MON; -.
DR UniPathway; UPA00344; -.
DR PRO; PR:O22827; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22827; baseline and differential.
DR Genevisible; O22827; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0019008; C:molybdopterin synthase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0030366; F:molybdopterin synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00756; MoaE; 1.
DR Gene3D; 3.90.1170.40; -; 1.
DR HAMAP; MF_03052; MOC2B; 1.
DR InterPro; IPR036563; MoaE_sf.
DR InterPro; IPR028888; MOCS2B_euk.
DR InterPro; IPR003448; Mopterin_biosynth_MoaE.
DR Pfam; PF02391; MoaE; 1.
DR SUPFAM; SSF54690; SSF54690; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Molybdenum cofactor biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..198
FT /note="Molybdopterin synthase catalytic subunit"
FT /id="PRO_0000369345"
FT BINDING 107..108
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT BINDING 130..132
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
SQ SEQUENCE 198 AA; 22216 MW; 7E9077839D05D585 CRC64;
MSAEEKNLIE ILEEGHKVDV VKYIDYVSAP QAGAIATFSG TTRDMFEGKT VLELRYEAYV
PMATRCLSSI CTTARSTWDI HKIAVAHRLG PVPVGETSVL IAVSSVHRAD GLDACKFLID
ELKASVPIWK KEVYTNGEIW KENSEFMEKR LELAEKRDSI VKKTVVEEHR RRGCCGSKVR
VEEDEEHKDI TGDNKSSS
