MOC2B_DROGR
ID MOC2B_DROGR Reviewed; 362 AA.
AC B4JHP4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
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=GH19575;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00;
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; CH916369; EDV93883.1; -; Genomic_DNA.
DR RefSeq; XP_001990821.1; XM_001990785.1.
DR AlphaFoldDB; B4JHP4; -.
DR SMR; B4JHP4; -.
DR STRING; 7222.FBpp0153481; -.
DR eggNOG; KOG3307; Eukaryota.
DR HOGENOM; CLU_045449_0_0_1; -.
DR InParanoid; B4JHP4; -.
DR OMA; GIAIYHR; -.
DR PhylomeDB; B4JHP4; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001070; Unassembled WGS sequence.
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:0006777; P:Mo-molybdopterin cofactor biosynthetic process; ISS:UniProtKB.
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..362
FT /note="Molybdopterin synthase catalytic subunit"
FT /id="PRO_0000369335"
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 362 AA; 41923 MW; 83DBDD454E430236 CRC64;
MDHIQLVNSQ IDINHIHNLL IDESCGASSV FVGTTRDNFD GKKVISLEYE SYEKMALKEM
SKICSQLRAR WPDLKHIAIY HRLGTVPVKE ASVVIATSAP HRAAALESVT FAVEQLKSRV
PIWKKEIYEN DTIGEWKENM ECPWPQYSKA SLRTFDFSSC KIKQTIENIP DKLVQIRVND
SDLNKRVKCF LKRKRDEINL HNINDFKQQS SQIPCEETTT FSCARTQSFL VKQQQSSGHL
KVRRANNCCG PQVRPNYSLQ LNKLMTPQSD CDDLIEYKLG NSRLRNIEAY MCVSPDDDNI
LNRIKNIEDR ILLIESTSPE YKHFVQFGTD SEKTCLKKPK KEVYLTDRIN EFLTKIKREI
EQ
