MOCOS_DROAN
ID MOCOS_DROAN Reviewed; 773 AA.
AC B3MZN7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Molybdenum cofactor sulfurase {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MCS {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MOS {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MoCo sulfurase {ECO:0000255|HAMAP-Rule:MF_03050};
DE EC=2.8.1.9 {ECO:0000255|HAMAP-Rule:MF_03050};
DE AltName: Full=Molybdenum cofactor sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03050};
DE AltName: Full=Protein maroon-like {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=Ma-l {ECO:0000255|HAMAP-Rule:MF_03050};
GN Name=mal {ECO:0000255|HAMAP-Rule:MF_03050}; ORFNames=GF19210;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13;
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: Sulfurates the molybdenum cofactor. Sulfation of molybdenum
CC is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase
CC (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and
CC 1 sulfur atom in active form. {ECO:0000255|HAMAP-Rule:MF_03050}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine +
CC thio-Mo-molybdopterin; Xref=Rhea:RHEA:42636, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:71302, ChEBI:CHEBI:82685; EC=2.8.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03050};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03050};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. MOCOS subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03050}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH902635; EDV33838.1; -; Genomic_DNA.
DR RefSeq; XP_001966793.1; XM_001966757.2.
DR AlphaFoldDB; B3MZN7; -.
DR SMR; B3MZN7; -.
DR STRING; 7217.FBpp0122402; -.
DR EnsemblMetazoa; FBtr0123910; FBpp0122402; FBgn0096221.
DR GeneID; 6501972; -.
DR KEGG; dan:6501972; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_1_1; -.
DR InParanoid; B3MZN7; -.
DR OMA; WCLVHQG; -.
DR OrthoDB; 394559at2759; -.
DR PhylomeDB; B3MZN7; -.
DR Proteomes; UP000007801; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; ISS:UniProtKB.
DR GO; GO:0102867; F:molybdenum cofactor sulfurtransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0043545; P:molybdopterin cofactor metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_03050; MOCOS; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR005302; MoCF_Sase_C.
DR InterPro; IPR028886; MoCo_sulfurase.
DR InterPro; IPR005303; MOSC_N.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR Pfam; PF00266; Aminotran_5; 2.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03476; MOSC_N; 1.
DR SUPFAM; SSF50800; SSF50800; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 3: Inferred from homology;
KW Molybdenum cofactor biosynthesis; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..773
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000369370"
FT DOMAIN 632..773
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT ACT_SITE 410
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 243
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 773 AA; 86857 MW; 58CF55C7B7FCC3E9 CRC64;
MTLYSPEFSE SEQSKIDAEF SRLTENKSVY LDHAGTTLYA ESQVKAAAEQ LQRNVICNPH
TCRLTGDFVD QVRYKVLEFF NTTSEDYHVI FTANATASLS LVAENFDFGS FGNFHFCQEN
HTSVLGMRER VSHAKGIYML TEREITGCSL QNGSSKEKPT DPGRSLVTFS AQCNFSGYKI
PLDAIGNIQE NGLHTPGKHI WGTEGKTSNN DYYICLDAAS FVATNPLDLK RYRPDFVCLS
FYKIFGYPTG VGALLVSKRG AEAFRDRKFF GGGTINYAYP HTMEYQLRES FHQRYEDGTL
PFLAIVGLLE GFRTLERIVP KTKELATMER ISRHVHGLAK YLEDQLKQLK HPNGEPLIQL
YNKAGYQDRT RQGGIVAFNV RTDSGDYVGF GEIACVAALH GILLRTGCFC NIGACQYYLG
LDGDAMDAIY KRAGRICGDY FDLIDGQPTG AVRVSFGYMT TIHDVEELLK MLRSSYLATK
PQQRILFIEE QAGQLPPVLQ KRVQNLRPKL LQMAIFPVKS CAAFKIEGYL KSWPLTDQGL
KYDREWMIVD MNGMALTQKR CTELCLIRPL IKNDVLELHF GDSCVSVPLS LEDQAADSAK
CVSKVCRQPV EGLDCGERVA EWLSTNLGQD GLRLLRQSGQ RNSSKDQQKL SLVNQAQFLL
VNRSSVRSLQ FEEPLDDTVD RFRANIIIDT GLAFEELSFK QLSIGKVQFQ VQGPCQRCDM
ICINQKTGER SPETLTTISR LQSGRMRFGI YITRISKDTG DLQLSCGDTV LVE
