ID W5P5X9_SHEEP Unreviewed; 849 AA.
AC W5P5X9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
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};
GN Name=MOCOS {ECO:0000256|HAMAP-Rule:MF_03050,
GN ECO:0000313|Ensembl:ENSOARP00000005832.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000005832.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000005832.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000005832.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000005832.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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=2 Fe(II)-[cytochrome b5] + 2 H(+) + N(omega)-hydroxy-L-
CC arginine = 2 Fe(III)-[cytochrome b5] + H2O + L-arginine;
CC Xref=Rhea:RHEA:61644, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:32682, ChEBI:CHEBI:60107;
CC Evidence={ECO:0000256|ARBA:ARBA00029322};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61645;
CC Evidence={ECO:0000256|ARBA:ARBA00029322};
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=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000256|ARBA:ARBA00001924};
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03050}.
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DR EMBL; AMGL01066141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01066142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01066143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01066144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5P5X9; -.
DR STRING; 9940.ENSOARP00000005832; -.
DR PaxDb; 9940-ENSOARP00000005832; -.
DR Ensembl; ENSOART00000005922.1; ENSOARP00000005832.1; ENSOARG00000005431.1.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_1_1; -.
DR OMA; PCTRCQM; -.
DR Proteomes; UP000002356; Chromosome 23.
DR Bgee; ENSOARG00000005431; Expressed in epididymis and 51 other cell types or tissues.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
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; IPR015422; PyrdxlP-dep_Trfase_small.
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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03050}.
FT DOMAIN 668..828
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT REGION 458..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 386
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ SEQUENCE 849 AA; 93850 MW; 0CB87B6784546A64 CRC64;
MQSRQSRALP PRPPGTVYLD HAGTTLFPQS QITSFMKDLM ENVYGNPHSQ NISSKLTHDT
VEQVRFRILA HFRTSPEDYT VIFTSGSTAA LKLVAEAFPW VSPGPEGSGS CFCYLTDSHT
SVVGMRKVTA ARDVTCIPVR PEDMWSAERQ DAAAAGDPAS QPPHLFCYPA QSNFSGTRYP
LSWIGEVQSG RRRPASRPGA WGLPPVGLCR GGGGWLELPQ QACVGLPQLW GSKGLPERAA
SRRHEALPGA GSEVFRGPDY LSGPLIITAR HKLQNRFEDG TISFLDVIAL KHGFDALERL
TGGMESIRQH TFTLAQYTYA ALSSLRYPNG APVVQIYSDS EFSSPEVQGP VISFNVLDDH
GNIVGYSQVD KMASLHNIHV RTGCFCNTGA CQRHLGISDE MVKKHLQAGH VCGDDVDLID
GQTTGCVRIS FGYMSTLEDA QAFLRFIIAT RLHPSHGQPL PLATPGEAGA PPGDSEAQNA
VPATWVRGSP SPQEDASPHS GVWNNSPTAF NAEDLCPPLL EATGPQQTTL ENAADIPDGD
LRSHVVTNLY LYPIKSCAAF EVTRWPLGSQ GLLYDRSWMV VNHNGICLSQ KQEPRLCLIQ
PFIDLQRRIM VIKAQGMEPI EVPLEENSEQ VRICQSKVCA DRVNTYDCGE KISNWLSKFF
GRPYHLIKQS SDFQRNAKKK HGKDQSARTT AALSLVNEAQ YLLINRSSIL ELQQQLSTSR
ENGKELFPMN NLISRFRANI ITNGTRAFEE EKWDEISVGS LRFQVLGPCH RCQMICIDQQ
TGQRNQDVFQ KLSERRERKV EFGVYLMHTS LDLSSPCYLS VGSQVLPLLK ENIEHHDIPA
TEKSQDAIS
//
