MOCO2_CULQU
ID MOCO2_CULQU Reviewed; 760 AA.
AC B0WSX1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Molybdenum cofactor sulfurase 2 {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MCS 2 {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MOS 2 {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MoCo sulfurase 2 {ECO:0000255|HAMAP-Rule:MF_03050};
DE EC=2.8.1.9 {ECO:0000255|HAMAP-Rule:MF_03050};
DE AltName: Full=Molybdenum cofactor sulfurtransferase 2 {ECO:0000255|HAMAP-Rule:MF_03050};
DE AltName: Full=Protein maroon-like 2 {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=Ma-l 2 {ECO:0000255|HAMAP-Rule:MF_03050};
GN Name=mal2 {ECO:0000255|HAMAP-Rule:MF_03050}; ORFNames=CPIJ009941;
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; EDS34099.1; -; Genomic_DNA.
DR RefSeq; XP_001870738.1; XM_001870703.1.
DR AlphaFoldDB; B0WSX1; -.
DR SMR; B0WSX1; -.
DR STRING; 7176.CPIJ009941-PA; -.
DR GeneID; 6042721; -.
DR KEGG; cqu:CpipJ_CPIJ009941; -.
DR VEuPathDB; VectorBase:CPIJ009941; -.
DR VEuPathDB; VectorBase:CQUJHB011474; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_1_1; -.
DR InParanoid; B0WSX1; -.
DR OMA; WCLVHQG; -.
DR OrthoDB; 394559at2759; -.
DR PhylomeDB; B0WSX1; -.
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; IPR020845; AMP-binding_CS.
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; 1.
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; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..760
FT /note="Molybdenum cofactor sulfurase 2"
FT /id="PRO_0000369369"
FT DOMAIN 608..758
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT ACT_SITE 389
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 223
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
SQ SEQUENCE 760 AA; 84400 MW; FD8B94CB4F87B4F2 CRC64;
MAMEQFESVF TAKENAEIAK EFTRLKDTCY LDHAGTTLYA DSQIRAVGDC LTGSLFCNPH
TSRTTEDLLD QVRFRVLRHF GTHPSEYGLV FTSGTTGALK LVAECFDFGD EGAFVYTRDN
HTSVLGMRAV VGTERIVPIG REDLRGGRST GGGKSSLVVF PAQCNFNGFK YPLGLVEDIQ
RNGLVGFDGD RFHVCLDAAS FVSTNALDLA KHQPSFVCLS FYKIFGFPTG LGALLVHRSA
QNLLKKRYYG GGTVKIAMAG RNFHVKRDSL ADQFEDGTVP FTSIISLLQG FETLERLVPA
SGELSSIDRV SRHTFALGRY CFQRLRGLRH ANSNSVVKLY HDTEFEDRGS QGGIVNFNVL
HEDGSFVGFA EVAYMASVHN VVLRTGCFCN PGACQRLLEL TDEDVLKQFN AGHVCGDAND
LIGGQPTGSV RVSFGYMSRR EDVDRLVEMV EKCYVKKMTA NGLTRKQIVS NYKNYDQPKL
KMICLFPIKS CGAYKITTSW PLCHKGLKHD REFVIVDENG VAMTQKKLVE MCLIKPKIDI
KTNTLILTHP AMENFTLSME PLSNESQSIK LCQTKVCQDN VQAIDCGDAV ANWISIALQT
SGLRLLKQSD DEARTLRKST TEIALSNQAQ FLLINQASVR WLADLVPDWD DLSQEPTLES
LVDRFRGNLI IDSVKPLEES SWTQLRIGPL EFSVDGPCSR CQMICIDQSS GTRTAEPLRT
IAREFKGKMR FGIYLSHVKS LEGSDEKLLH CGSPLQVVAE
