MOC2B_DROMO
ID MOC2B_DROMO Reviewed; 366 AA.
AC B4KBH3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=GI23778;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22;
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; CH933806; EDW13640.1; -; Genomic_DNA.
DR AlphaFoldDB; B4KBH3; -.
DR SMR; B4KBH3; -.
DR STRING; 7230.FBpp0172995; -.
DR EnsemblMetazoa; FBtr0429167; FBpp0386649; FBgn0281273.
DR eggNOG; KOG3307; Eukaryota.
DR HOGENOM; CLU_045449_0_0_1; -.
DR InParanoid; B4KBH3; -.
DR OMA; GIAIYHR; -.
DR OrthoDB; 1543738at2759; -.
DR PhylomeDB; B4KBH3; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000009192; 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..366
FT /note="Molybdopterin synthase catalytic subunit"
FT /id="PRO_0000369337"
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 366 AA; 42765 MW; 315DA9F1611B9C13 CRC64;
MDHIKLIRNK IDINHIHQLI IDQSCGACSV FVGTTRDHFE GKKVISLEYE AYESMALKEM
GKICSELRIR WPTLKHIAIY HRLGSVPVAE ESVVIAVSAP HRPAALESVS FAVDKLKSSV
PIWKKEIYEN DQIGEWKANM ECPWPQFTET SSNAFEYSLC KIERQVENIS ESKLVQIRVS
DIELTRRIKC FLKRKRDEIN LHNIIDFKQQ LRDSPRAESM LPKDSCARTQ SILVKQQQSI
SHIKVHRAFE DRRQTRPDYS SQLNKLMATK HKHCELVKSN VLKNARLQNI EEYMRITPDD
EDNIYNRIKN IENRILILES TSPEYKYYIK LGKESNNINK KESKKGLYQS DRLSEFISGI
KRQYEL
