MOCOS_NEOFI
ID MOCOS_NEOFI Reviewed; 851 AA.
AC A1CX75;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Molybdenum cofactor sulfurase {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MCS {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MOS {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MoCo sulfurase {ECO:0000255|HAMAP-Rule:MF_03050};
DE EC=2.8.1.9 {ECO:0000255|HAMAP-Rule:MF_03050};
DE AltName: Full=Molybdenum cofactor sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03050};
GN Name=hxB {ECO:0000255|HAMAP-Rule:MF_03050}; ORFNames=NFIA_107180;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027685; EAW25227.1; -; Genomic_DNA.
DR RefSeq; XP_001267124.1; XM_001267123.1.
DR AlphaFoldDB; A1CX75; -.
DR SMR; A1CX75; -.
DR STRING; 36630.CADNFIAP00009354; -.
DR EnsemblFungi; EAW25227; EAW25227; NFIA_107180.
DR GeneID; 4593751; -.
DR KEGG; nfi:NFIA_107180; -.
DR VEuPathDB; FungiDB:NFIA_107180; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_0_1; -.
DR OMA; WCLVHQG; -.
DR OrthoDB; 394559at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
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; -; 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..851
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000369385"
FT DOMAIN 665..844
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT ACT_SITE 413
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 249
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
SQ SEQUENCE 851 AA; 95040 MW; A4A3248B734A8AD3 CRC64;
MEGDTRRMWT QSESESIRSS KVRPLPLRKV TLYLTFVLIG VADTTYLDHA GTTLYAKSLI
ESFSRELTSN LFGNPHSLSA SSQLSTRRVD DVRLRALRFF KADPDEFDLV FVANATAAIK
LVADGMRDST RQGFWYGYHV DAHTSLVGVR ELAEKGGRCF TSDDEVEDWI SKLCDVRSES
LKLFAYPAQS NMNGRRLPLS WCKKIRNQGE TAGGNVYTLL DAASLVSTST LDLSDAAAAP
DFTVLSFYKI FGFPDLGALI VRKSAGQIFE HRRYFGGGTV DMVLTRGLQW HAKKQSSIHD
RLEDGTLPFH DIIALDSAFA THERLFGSMQ NISSHTRFLA KRLYDRLNAL RHFNGQRVCE
LYKSPRSDYN QPSTQGPIIA FNLRNSQGSW IGKSEVERLA AMRNIQIRSG SLCNPGGTSG
SLGWTGADLL QQFSAGLRCG DDHDVMDGRP TGVLRLSLGA MTNLEDINTF VEFVEEFYVE
KVATMDSLVT PVHSVPLQQP RFYIESLSLY PIKSCGPFRV PDGRRWEVRR EGLAWDREWC
LIHQGTGAAL NQKKYPRMAL IRPSIDLDRN VLRVTCEEPG STNQKLLEVS LLREDTELAT
TSLCQRTSKA STVCGDQVTV QAYTSPSVAQ FFSDFLGVPC TLARFGPHSS TRYASPRKAP
GAWKQYLRKF VMPGSFPQEP SPPPAEKNPI LLSNESPILL ISRSSVNHLN ENIKANQKRN
RTGTSKAVAA DVFRANIVVA ESLADSPKVE QPYIEDQWEA LKIGPGELQF DVLGSCQRCS
MVCIDQFTGV RRDEPFSTLA KTRKINNKIV FGRHCSLSAS EVTKEQHDNA ERWTLMVGDI
VTPSYAHDYD L
