MOC2A_CAEEL
ID MOC2A_CAEEL Reviewed; 84 AA.
AC Q09412;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Molybdopterin synthase sulfur carrier subunit {ECO:0000255|HAMAP-Rule:MF_03051};
DE AltName: Full=Molybdenum cofactor synthesis protein 2 small subunit {ECO:0000255|HAMAP-Rule:MF_03051};
DE AltName: Full=Molybdenum cofactor synthesis protein 2A {ECO:0000255|HAMAP-Rule:MF_03051};
DE Short=MOCS2A {ECO:0000255|HAMAP-Rule:MF_03051};
DE AltName: Full=Sulfur carrier protein MOCS2A {ECO:0000255|HAMAP-Rule:MF_03051};
GN ORFNames=K10D2.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Acts as a sulfur carrier required for molybdopterin
CC biosynthesis. Component of the molybdopterin synthase complex that
CC catalyzes the conversion of precursor Z into molybdopterin by mediating
CC the incorporation of 2 sulfur atoms into precursor Z to generate a
CC dithiolene group. In the complex, serves as sulfur donor by being
CC thiocarboxylated (-COSH) at its C-terminus by MOCS3. After interaction
CC with MOCS2B, the sulfur is then transferred to precursor Z to form
CC molybdopterin. {ECO:0000255|HAMAP-Rule:MF_03051}.
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03051}.
CC -!- SUBUNIT: Heterotetramer; composed of 2 small (MOCS2A) and 2 large
CC (MOCS2B) subunits. {ECO:0000255|HAMAP-Rule:MF_03051}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03051}.
CC -!- PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-
CC adenylated (-COAMP) via the hesA/moeB/thiF part of MOCS3, then
CC thiocarboxylated (-COSH) via the rhodanese domain of MOCS3.
CC {ECO:0000255|HAMAP-Rule:MF_03051}.
CC -!- SIMILARITY: Belongs to the MoaD family. MOCS2A subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03051}.
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DR EMBL; FO081618; CCD72862.1; -; Genomic_DNA.
DR PIR; F88451; F88451.
DR RefSeq; NP_498102.1; NM_065701.4.
DR AlphaFoldDB; Q09412; -.
DR SMR; Q09412; -.
DR BioGRID; 51967; 1.
DR STRING; 6239.K10D2.7; -.
DR EPD; Q09412; -.
DR PaxDb; Q09412; -.
DR PeptideAtlas; Q09412; -.
DR EnsemblMetazoa; K10D2.7.1; K10D2.7.1; WBGene00019633.
DR GeneID; 187263; -.
DR KEGG; cel:CELE_K10D2.7; -.
DR UCSC; K10D2.7; c. elegans.
DR CTD; 187263; -.
DR WormBase; K10D2.7; CE02019; WBGene00019633; -.
DR eggNOG; KOG3474; Eukaryota.
DR HOGENOM; CLU_114601_4_3_1; -.
DR InParanoid; Q09412; -.
DR OMA; DQEYANP; -.
DR OrthoDB; 1631547at2759; -.
DR PhylomeDB; Q09412; -.
DR UniPathway; UPA00344; -.
DR PRO; PR:Q09412; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00019633; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.10.20.30; -; 1.
DR HAMAP; MF_03051; MOCS2A; 1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR044672; MOCS2A.
DR InterPro; IPR028887; MOCS2A_euk.
DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR InterPro; IPR003749; ThiS/MoaD-like.
DR PANTHER; PTHR33359; PTHR33359; 1.
DR Pfam; PF02597; ThiS; 1.
DR SUPFAM; SSF54285; SSF54285; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Molybdenum cofactor biosynthesis; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..84
FT /note="Molybdopterin synthase sulfur carrier subunit"
FT /id="PRO_0000065408"
FT MOD_RES 84
FT /note="1-thioglycine; alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03051"
FT MOD_RES 84
FT /note="Glycyl adenylate; alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03051"
SQ SEQUENCE 84 AA; 9595 MW; 777A5E40F949BA39 CRC64;
MISIKVLFFG EACQLVGKRE EAIDFPEETD YEEIRKTILE NYPALQKIEK VMMLAVDQEY
ANPGDRFELV RFTEIAVIPP LSGG
