MOCOS_MAGO7
ID MOCOS_MAGO7 Reviewed; 842 AA.
AC A4RK48; G4MTZ6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 25-MAY-2022, entry version 86.
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=MGG_01613;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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; CM001232; EHA54790.1; -; Genomic_DNA.
DR RefSeq; XP_003714597.1; XM_003714549.1.
DR AlphaFoldDB; A4RK48; -.
DR SMR; A4RK48; -.
DR STRING; 318829.MGG_01613T0; -.
DR EnsemblFungi; MGG_01613T0; MGG_01613T0; MGG_01613.
DR GeneID; 2679314; -.
DR KEGG; mgr:MGG_01613; -.
DR VEuPathDB; FungiDB:MGG_01613; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_0_1; -.
DR InParanoid; A4RK48; -.
DR OMA; WCLVHQG; -.
DR OrthoDB; 394559at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
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; Reference proteome;
KW Transferase.
FT CHAIN 1..842
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000369384"
FT DOMAIN 663..831
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT REGION 637..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 402
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 236
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
SQ SEQUENCE 842 AA; 91875 MW; 8510E929C74988CB CRC64;
MAQNLDAQYN AAVERFRSEE FPMIRVDSIY LDHAGTTLCP KSLLEAFARD MAGNLYGNPH
SASNSSQLST SRIEDIRLQA LQLFGASPDE FDLVFVANAT AGIKLVSESL RARDGGFGFL
YHQASHTSLV GVREEAQSSI CLSEDETEEL LAGSTTSLDL VTRSPPGAVL LAYTAQSNFD
GRRYPLTWAD KVRRAHASGC TPICTLLDAA SFVSTSPLHL GESKAAPDFT VLSFYKIFGF
PDLGALIVRK QAWHLFESRK YFGGGTVDMV VNFKESWHAP KNGFLHERLE DGTLPIHNIL
ALGSAIKIHQ GLFGPMRTVS SHATFLAQEM ITNLQNLHHS NGEKVCTLYS PYPKPNVDGN
GWNQGPIIAF NICTSNGSWV SLGEFEKLAS LRDINIRTGS LCNPGGIAIA LALEPWEMKR
NFSAGLRCGA DNDMALGKPT GVIRASLGAM STTSDVDRFV AFIVEFFCDD GAASRDLQTP
RVQPSLASGE AELCVDSLTI YPIKSCAGYS IPHGKQWQVR PEGLAWDREW CLLHRGSGQA
LSQKRYPKMA LIKPVVDLES GRLAVGYLGE PIPYLPERVS VPLSHDPSVF RPSTYVSAAP
SRVCGDQVAT KIYHDDELNE FFSKAIGVPC VLARFPPGSQ HGDAQRSSKA RLQKHQITTD
QESDVQEVHP GSGTTTDSTW GNDKSQNILL SNESPILLIN LASVDALNQE IKSRKGSSAV
RIPTSAFRAN VVLRRTDESR PDGAQGLPYA EERWRGLTIG NQTYTMLGAC RRCQMVCVDQ
VTGCRGDEPF STLSKTRRFD GKVFFGVHMA WGPGSPSNNV VAARGDVAYP TIEVGERVLV
HV
