MOCOS_BOTFB
ID MOCOS_BOTFB Reviewed; 813 AA.
AC A6SRX6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=BC1G_15280;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH477024; EDN22629.1; -; Genomic_DNA.
DR RefSeq; XP_001545952.1; XM_001545902.1.
DR AlphaFoldDB; A6SRX6; -.
DR SMR; A6SRX6; -.
DR PRIDE; A6SRX6; -.
DR GeneID; 5426407; -.
DR KEGG; bfu:BCIN_01g03840; -.
DR VEuPathDB; FungiDB:Bcin01g03840; -.
DR OMA; WCLVHQG; -.
DR OrthoDB; 394559at2759; -.
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 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 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; Transferase.
FT CHAIN 1..813
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000369382"
FT DOMAIN 648..812
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT REGION 625..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 391
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 813 AA; 90173 MW; AF92BFB081E10F81 CRC64;
MEEYNKAVEE FRKHEYPMLK DAVYLDHAGT TLYSKSLMER YMGDMMSNLY GNPHSASTSS
QLSTSRIENT RLNVLQFFNA DPEDFDVVFV ANATAGIKLV MDAFRCQEDG FLYGYHQDSH
TSLVGVREDA VSSRCLDDDA VECWLSGSEA LVRNEHNSEI GLFAYPAQSN LDGRRLPLSW
PERVRNLSYE AQANTYTLLD ASALVSTSPL DLSDVSKAPD FTVLSFYKIF GFPDLGALIV
RKDSGAILQT RKYFGGGTVE VVVCLKEQWH APKGQSLHEN LEDGTLPFHN IMALEAAIDV
HKSLYGSMEC IANHTTFLAR KLYEGLKSLQ HANSEPACII YSPGFSETSS NVQGPTIAFN
VKNSFGAWVT NVEFERLASI KNYHIRTGGL CNPGGVASAL ELQPWETRRN FSAGLRCGGE
TDIYAGKITG VIRVSLGAMS TMSDVDSFLS FVNEFFVDHT VVSADEDGES QKSVDMYVES
LTIYPIKSCG GFEIPKETAW EVRPEGLAWD REWCLIHQGT GQALSQKRYP RMALIKPTID
FDLGLLKLRY QGSTFPTLVD EISVSLSSDP SSYKNPNNIH SLSSRVCGDA IAAQTYFDHE
INDFFSKILE APCVLARFPA GGSGPSLRHA KAHMQKHQGP KRSAAIEKSS AHSFHDPPTP
PDSDSENRKR PILLSNESPI LAINRSSINM LNEEIAKSGG KLASASVFRG NIVLASTELT
DSHHPYSEDH WSTLQIGSET YQMLGSCRRC HMICVDQDTA EKNEEPFVTL AKTRRFESKV
FFGSHMCHVP SFSRHKKHQF PVIKVGDKVS IGL
