MOC2B_DROER
ID MOC2B_DROER Reviewed; 367 AA.
AC B3P6R5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-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=GG12284;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01;
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: 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; CH954182; EDV53735.1; -; Genomic_DNA.
DR RefSeq; XP_001981865.1; XM_001981829.2.
DR AlphaFoldDB; B3P6R5; -.
DR SMR; B3P6R5; -.
DR STRING; 7220.FBpp0130830; -.
DR EnsemblMetazoa; FBtr0132338; FBpp0130830; FBgn0104575.
DR GeneID; 6555340; -.
DR KEGG; der:6555340; -.
DR eggNOG; KOG3307; Eukaryota.
DR HOGENOM; CLU_045449_0_0_1; -.
DR OMA; GIAIYHR; -.
DR OrthoDB; 1543738at2759; -.
DR PhylomeDB; B3P6R5; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000008711; 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; Transferase.
FT CHAIN 1..367
FT /note="Molybdopterin synthase catalytic subunit"
FT /id="PRO_0000369334"
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; 42049 MW; 1C291A71513D912E CRC64;
MDHVKLVNDP IDIAHIHQLL ADAGCGASSV FVGTTRDNFQ GKKVVSLAYE AYDSMALKEM
NKICLDLRSK WPDLKHIVIY HRLGTVPVCE ASVVIAASSP HRSEALESVS FAIDQLKTRV
PIWKKEIYEG DHVSEWKENK ESIRPKRSKS AFNYAACPCK VEESHDVPRT LVQIRVNDAE
LTKRLECFVN RKRDEINSQN VIDFKSSFVN SDIDLSDSCA RTQSTIIKQE QSNCHLKVRR
VNNRCGPQQM EMRPNYELEL NKLMGSRDGQ TDPFKEMRKS LPNSRLQAIE SYMCLTTDNE
ENIFSRIKKV ENRLLQLESI SPEYRHFTKL EPSSMELPPP KKIRKKSYSV PELSAFIQKI
KEGSEFA