ID   MOC2B_DROSE             Reviewed;         367 AA.
AC   B4IJG7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 59.
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=Mocs2B {ECO:0000250|UniProtKB:Q9VBX2};
GN   Synonyms=Mocs2 {ECO:0000255|HAMAP-Rule:MF_03052}; ORFNames=GM17748;
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25;
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: 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   -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC       also produces the small subunit (Mocs2A).
CC   -!- SIMILARITY: Belongs to the MoaE family. MOCS2B subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03052}.
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DR   EMBL; CH480848; EDW51158.1; -; Genomic_DNA.
DR   RefSeq; XP_002043877.1; XM_002043841.1.
DR   AlphaFoldDB; B4IJG7; -.
DR   SMR; B4IJG7; -.
DR   STRING; 7238.B4IJG7; -.
DR   EnsemblMetazoa; FBtr0200733; FBpp0199225; FBgn0172656.
DR   GeneID; 6619662; -.
DR   KEGG; dse:6619662; -.
DR   HOGENOM; CLU_045449_0_0_1; -.
DR   OMA; GIAIYHR; -.
DR   PhylomeDB; B4IJG7; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001292; Unassembled WGS sequence.
DR   GO; GO:0140672; C:ATAC complex; IEA:EnsemblMetazoa.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0019008; C:molybdopterin synthase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005700; C:polytene chromosome; IEA:EnsemblMetazoa.
DR   GO; GO:0030366; F:molybdopterin synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:EnsemblMetazoa.
DR   GO; GO:0016573; P:histone acetylation; IEA:EnsemblMetazoa.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IEA:EnsemblMetazoa.
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   3: Inferred from homology;
KW   Cytoplasm; Molybdenum cofactor biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN           1..367
FT                   /note="Molybdopterin synthase catalytic subunit"
FT                   /id="PRO_0000369340"
FT   REGION          326..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         101..102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT   BINDING         124..126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
SQ   SEQUENCE   367 AA;  41921 MW;  E43C9BB4B606109D CRC64;
     MDHVKLVNDP IDIAHIHQLL ADEGCGASSV FVGTTRDNFQ GKKVLSLAYE AYDSMALKEM
     NKICSDLRSK WLDLKHIVIY HRLGTVPVCQ ASVVIAASSP HRSEALESVS FAIDQLKTRV
     PIWKKEIYEG DNDSEWKENK ESIRPKKSKS GFNYAACPCK VEESHDVPRT LVQIRVNDAE
     LAKRLECFVN RKRDEINSQN VIDFKSSFVS SDKDLSDSCA RTQSTIIKQE QSNCHLKVRR
     VNNRCGPQQM EMRPNYELEL NKLMGSRDGQ TDPTKEMRKS LPNSRLQAIE SYMGLTTDNE
     ENIFSRIKRV ENRLLQLESI SPEYRHFTKR EPSSMEAAPP KKIRKKSYSA QELSAFIQKV
     KDGSEFS