MOCO1_AEDAE
ID MOCO1_AEDAE Reviewed; 764 AA.
AC Q16GH0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=AAEL014381;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(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}.
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DR EMBL; CH478278; EAT33329.1; -; Genomic_DNA.
DR RefSeq; XP_001648634.1; XM_001648584.1.
DR AlphaFoldDB; Q16GH0; -.
DR SMR; Q16GH0; -.
DR STRING; 7159.AAEL014381-PA; -.
DR VEuPathDB; VectorBase:AAEL022615; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_1_1; -.
DR InParanoid; Q16GH0; -.
DR OMA; AANEHRI; -.
DR PhylomeDB; Q16GH0; -.
DR Proteomes; UP000008820; 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: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 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..764
FT /note="Molybdenum cofactor sulfurase 1"
FT /id="PRO_0000369364"
FT DOMAIN 607..762
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT ACT_SITE 394
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 228
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
SQ SEQUENCE 764 AA; 86630 MW; E2DFA9E1D4D38385 CRC64;
MEAMMNFTSQ YTVEEALAIE NEFSRLKEKC YLDHAGTTLY ADSQIRSVCE GLAQNLYCNP
HTSRTTEDLL DQVRYRVLRH FNTRSSEYSL IFTSGTTASL KLLAESFEFA PEGAFVYLKD
SHTSVLGMRE IVGTERIYPV EREQLLKELD SSERSDNEHS SLIVFPAQCN FNGVKYPLEL
VRKIQRDGIS GYGKERFRVC LDAASFVSTS FLDLSKYQPD FVCLSFYKIF GYPTGLGALL
VHHTAADQLR KKYYGGGTVK IAMAGRIFHV KRDPLVERFE DGTLAFTSII ALLQGFETLE
RLVPSTAGLR TIERISQQTF HIGRYCYNRL KALRHSNENA VVKLYHDTGF EDRGLQGGIV
NFNILHEDGT YVGFAEVSYM ASLHNILLRT GCFCNPGACQ RHLQLSDEDV LKQFDAGHVC
GDANDLIDGQ PTGSVRVSFG YMTRKEDIDC LLEMIEKCYI RKTIANGFTR TQIVSKYKSH
DQPRLKMICL FPIKSCGAFK VTTRWPLSRR GLKHDREFVI VDENGVALTQ KKLAEMCLIR
PQINVKTNEM TLSHPGMADF VLQLDLLGES QRIKLCQTKV CQDNVQAIDC GDQVAEWISV
ALQTSGLRLL KQSDEEVRTF QQSKQEIALA NQAQFLLINQ ASVRWLADKV PDWDELHEEP
TLESLVDRFR GNLIVETPKS MEECDWKRVT IGYLEFAVDG PCSRCQMICI DQGTGVKATE
PLRTIGREFK GKMRFGIYLS HVNPLRDGSE QWLYCNSVVE GLSE
