ID A0A1I8HIL3_9PLAT Unreviewed; 766 AA.
AC A0A1I8HIL3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Molybdenum cofactor sulfurase {ECO:0000256|HAMAP-Rule:MF_03050};
DE Short=MCS {ECO:0000256|HAMAP-Rule:MF_03050};
DE Short=MOS {ECO:0000256|HAMAP-Rule:MF_03050};
DE Short=MoCo sulfurase {ECO:0000256|HAMAP-Rule:MF_03050};
DE EC=2.8.1.9 {ECO:0000256|HAMAP-Rule:MF_03050};
DE AltName: Full=Molybdenum cofactor sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_03050};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0006245-snap-gene-0.3-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0006245-snap-gene-0.3-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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:0000256|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:0000256|HAMAP-Rule:MF_03050};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03050};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. MOCOS subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_03050}.
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DR AlphaFoldDB; A0A1I8HIL3; -.
DR WBParaSite; maker-uti_cns_0006245-snap-gene-0.3-mRNA-1; maker-uti_cns_0006245-snap-gene-0.3-mRNA-1; maker-uti_cns_0006245-snap-gene-0.3.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; IEA:UniProtKB-UniRule.
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 Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; MOCOS_middle.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR PANTHER; PTHR14237:SF19; MOLYBDENUM COFACTOR SULFURASE; 1.
DR PANTHER; PTHR14237; MOLYBDOPTERIN COFACTOR SULFURASE MOSC; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03476; MOSC_N; 1.
DR SUPFAM; SSF141673; MOSC N-terminal domain-like; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 3: Inferred from homology;
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|HAMAP-Rule:MF_03050};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_03050};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03050}.
FT DOMAIN 614..766
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT ACT_SITE 379
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
FT MOD_RES 215
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ SEQUENCE 766 AA; 83606 MW; BA7E9AA45E8D72E5 CRC64;
MDVRQLRQLE FPQLNDYVYL DHAGATLYSE RQLTRVMQEL QSGLYGNPHT QARKSAHTSR
LVEEARNSVL KHFNTSNQQH AVIFTSGATA AVKILAESFQ AGQHGAGLFN YLLDSHTSIV
GMREVLRSRG FVVRCSRTEL ELESATSSSS DGRVLFALPA QCNFSGRKLD LSIVDRLKAN
NKDAYVLLDA ASFAATCPLD LTACSADFVC LSFYKMFGYP TGLGALIVRL DRVANGESVL
KKAYFGGGTV QAMVPSGSFV QQSPDLAAGF EDGTINYLSI LAVRHGLWAL EQLGGGMQQI
SQRVFRLAQY LARRLSELRH SDGSPVCLLY TDNDYTDWTK QGGIVAFNLV RCDGSFVGYS
DLSSRAENYR IQLRVGCFCN VGACQRYLDI TDEQLLANLR AGHVCGDGVD LVDGRPTGAV
RASFGYMSDE SDADALVAMV TDNFVITKPM PVFSAAAASA PLMSMSRDEL ANLCRGGQSA
ASKAAAESHW PHLGRIFLYP VKSCAAFEVA ASWPVDRRGF HLDRHWMVVN ESGLCLTMKR
EPRLSQIRPF LDLQRRLLIL NSPISDQNAV VPMDAGHQTA ALCLHSRVCG SRVRLLDCGQ
AAADWLHSVV GYPCRLVRQD GDRLAKTGEQ AISLANEQQF LLLNEASVAH LLDCIGPESP
LDLSQLVARF RANLVVRGCQ PMSEESWTRL SIGGRQFAAH GVCTRCDMIG IDQDTGESTI
EPMRTLSQMK GGALKFGLYV SATASDNTTD KAAKFELSVG DAVIAE
//