MOC2A_DROYA
ID MOC2A_DROYA Reviewed; 90 AA.
AC B4PUD0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
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 Name=Mocs2A {ECO:0000250|UniProtKB:P0C919};
GN Synonyms=Mocs2 {ECO:0000255|HAMAP-Rule:MF_03051}; ORFNames=GE10736;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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 -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC also produces the large subunit (Mocs2B).
CC -!- SIMILARITY: Belongs to the MoaD family. MOCS2A subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03051}.
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DR EMBL; CM000160; EDW98817.1; -; Genomic_DNA.
DR RefSeq; XP_002099105.1; XM_002099069.2.
DR AlphaFoldDB; B4PUD0; -.
DR SMR; B4PUD0; -.
DR STRING; 7245.FBpp0255746; -.
DR EnsemblMetazoa; FBtr0257254; FBpp0255746; FBgn0228579.
DR GeneID; 6538583; -.
DR KEGG; dya:Dyak_GE10736; -.
DR eggNOG; KOG3474; Eukaryota.
DR HOGENOM; CLU_114601_4_3_1; -.
DR OMA; HVLFFAK; -.
DR OrthoDB; 1631547at2759; -.
DR PhylomeDB; B4PUD0; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000002282; Chromosome 3R.
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.
FT CHAIN 1..90
FT /note="Molybdopterin synthase sulfur carrier subunit"
FT /id="PRO_0000369315"
FT MOD_RES 90
FT /note="1-thioglycine; alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03051"
FT MOD_RES 90
FT /note="Glycyl adenylate; alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03051"
SQ SEQUENCE 90 AA; 9871 MW; 3E43683CE6D0D96F CRC64;
MNADGPVVNV HVLFFAKSRE LANTPRSKVD LPTEITASDL LELLVSKFGL TPIRDNLILA
HNESYIDNLS ERILFKEGDE LAIIPPLSGG
