MOCO1_CULQU
ID MOCO1_CULQU Reviewed; 759 AA.
AC B0WSW8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Molybdenum cofactor sulfurase 1 {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MCS 1 {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MOS 1 {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MoCo sulfurase 1 {ECO:0000255|HAMAP-Rule:MF_03050};
DE EC=2.8.1.9 {ECO:0000255|HAMAP-Rule:MF_03050};
DE AltName: Full=Molybdenum cofactor sulfurtransferase 1 {ECO:0000255|HAMAP-Rule:MF_03050};
DE AltName: Full=Protein maroon-like 1 {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=Ma-l 1 {ECO:0000255|HAMAP-Rule:MF_03050};
GN Name=mal1 {ECO:0000255|HAMAP-Rule:MF_03050}; ORFNames=CPIJ009938;
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB;
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; DS232077; EDS34096.1; -; Genomic_DNA.
DR RefSeq; XP_001870735.1; XM_001870700.1.
DR AlphaFoldDB; B0WSW8; -.
DR SMR; B0WSW8; -.
DR STRING; 7176.CPIJ009938-PA; -.
DR GeneID; 6042718; -.
DR KEGG; cqu:CpipJ_CPIJ009938; -.
DR VEuPathDB; VectorBase:CPIJ009938; -.
DR VEuPathDB; VectorBase:CQUJHB010643; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_1_1; -.
DR InParanoid; B0WSW8; -.
DR OMA; NNFNAAK; -.
DR OrthoDB; 394559at2759; -.
DR PhylomeDB; B0WSW8; -.
DR Proteomes; UP000002320; Partially assembled 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:0044248; P:cellular catabolic process; IEA:UniProt.
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 GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
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 Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03476; MOSC_N; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 3: Inferred from homology;
KW Molybdenum cofactor biosynthesis; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..759
FT /note="Molybdenum cofactor sulfurase 1"
FT /id="PRO_0000369368"
FT DOMAIN 591..738
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT ACT_SITE 397
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 231
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
SQ SEQUENCE 759 AA; 84929 MW; 4909E8662988C96A CRC64;
MEFVQEYSDE EAAAIEREFT RLKDKHYLDH GGATLYAESQ IQAVHDLLTA NMFGNPHTSH
QTGQLMDEVR RRVLRFFNTD SSEYSLIFTS GATASLKMVA ENFTFRAADS AEGDEGAFVY
LRDNHTSVLG MRAIVGTSRI HPLERENFVR HLKVSARSSQ RKPSLVVFPA QNNFNAAKYP
LELIEEIREN GLVGYDDDKF YVCLDVASFV STNFLDLDRY KPDFVCMSFY KIFGYPTGLG
ALLIRKGSED LLDKKYYGGG TIQIVMSGKN LHRKHVKPSD CFEDGTQPFL SIIALLEGFN
TIQRLIPPSN GYRSMERVSK HVFNLAKYCY HQLGELVHAN GAKVIHFYMD SRFESRDRQG
GIVTFNVLKD DGSYVGYAEF ARIALKHAVY LRAGCFCNSG TCQRQLKLSD EGLLEYFKMG
KICGDDNDMI DGHPTGTVRA AFGYMTKPEN VDRLVEMIRE RFVSQGISRP VKPTNRSSND
EELELKAIYI YPIRSCGSFT VTTSWPMVDR GLKHDREFSI VNSNGTPLSQ SKHTDMASIV
PKIDPRSNVL ILTHPTMPDL ILNLNKLPTA KSTILPEDSV DCGDEIAAWI SKALRQPRLR
LAKHLNDGNH SPPPKILMIN GNALRSLGDE DSAEDQATAS WLVEHFQGNL VVEAPATVDM
QTWKQVAIGE HRFKVVGMCT RCPMIYVDPA SGKVSADSLK AIANVFKKKV PLGMYLAYVG
DGGATARSLQ CGGRFILEQK DHSKVTSITE SVVRFNFNG
