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Database: UniProt
Entry: R0I5T6_SETT2
LinkDB: R0I5T6_SETT2
Original site: R0I5T6_SETT2 
ID   R0I5T6_SETT2            Unreviewed;       825 AA.
AC   R0I5T6;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   05-DEC-2018, entry version 29.
DE   RecName: Full=Molybdenum cofactor sulfurase {ECO:0000256|HAMAP-Rule:MF_03050};
DE            Short=MCS {ECO:0000256|HAMAP-Rule:MF_03050};
DE            Short=MOS {ECO:0000256|HAMAP-Rule:MF_03050};
DE            Short=MoCo sulfurase {ECO:0000256|HAMAP-Rule:MF_03050};
DE            EC=2.8.1.9 {ECO:0000256|HAMAP-Rule:MF_03050};
DE   AltName: Full=Molybdenum cofactor sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_03050};
GN   Name=hxB {ECO:0000256|HAMAP-Rule:MF_03050};
GN   ORFNames=SETTUDRAFT_174644 {ECO:0000313|EMBL:EOA80990.1};
OS   Setosphaeria turcica (strain 28A) (Northern leaf blight fungus)
OS   (Exserohilum turcicum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Pleosporaceae; Exserohilum.
OX   NCBI_TaxID=671987 {ECO:0000313|EMBL:EOA80990.1, ECO:0000313|Proteomes:UP000016935};
RN   [1] {ECO:0000313|EMBL:EOA80990.1, ECO:0000313|Proteomes:UP000016935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=28A {ECO:0000313|Proteomes:UP000016935};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A.,
RA   Barry K.W., Condon B.J., Copeland A.C., Dhillon B., Glaser F.,
RA   Hesse C.N., Kosti I., LaButti K., Lindquist E.A., Lucas S.,
RA   Salamov A.A., Bradshaw R.E., Ciuffetti L., Hamelin R.C., Kema G.H.J.,
RA   Lawrence C., Scott J.A., Spatafora J.W., Turgeon B.G.,
RA   de Wit P.J.G.M., Zhong S., Goodwin S.B., Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in
RT   the genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|EMBL:EOA80990.1, ECO:0000313|Proteomes:UP000016935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=28A {ECO:0000313|Proteomes:UP000016935};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R.,
RA   Martin J., Schackwitz W., Grimwood J., MohdZainudin N., Xue C.,
RA   Wang R., Manning V.A., Dhillon B., Tu Z.J., Steffenson B.J.,
RA   Salamov A., Sun H., Lowry S., LaButti K., Han J., Copeland A.,
RA   Lindquist E., Barry K., Schmutz J., Baker S.E., Ciuffetti L.M.,
RA   Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector
RT   coding capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
CC   -!- FUNCTION: Sulfurates the molybdenum cofactor. Sulfation of
CC       molybdenum is essential for xanthine dehydrogenase (XDH) and
CC       aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is
CC       liganded by 1 oxygen and 1 sulfur atom in active form.
CC       {ECO:0000256|HAMAP-Rule:MF_03050}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine
CC         + thio-Mo-molybdotperin; Xref=Rhea:RHEA:42636,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:57972, ChEBI:CHEBI:71302,
CC         ChEBI:CHEBI:82685; EC=2.8.1.9; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03050};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03050};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. MOCOS subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_03050}.
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DR   EMBL; KB908877; EOA80990.1; -; Genomic_DNA.
DR   RefSeq; XP_008031557.1; XM_008033366.1.
DR   EnsemblFungi; EOA80990; EOA80990; SETTUDRAFT_174644.
DR   GeneID; 19401338; -.
DR   OrthoDB; EOG092C1E70; -.
DR   Proteomes; UP000016935; 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   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; 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   Complete proteome {ECO:0000313|Proteomes:UP000016935};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|HAMAP-Rule:MF_03050};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_03050};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016935};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03050}.
FT   DOMAIN      649    809       MOSC. {ECO:0000259|PROSITE:PS51340}.
FT   ACT_SITE    390    390       {ECO:0000256|HAMAP-Rule:MF_03050}.
FT   MOD_RES     226    226       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03050}.
SQ   SEQUENCE   825 AA;  90844 MW;  71FDF6AF443587A6 CRC64;
     MDEAECIRYN SAIQQLRTRE YPMLQDTTYL DHAGTTLYSK SLMERFSADM VANLYGNPHS
     ASNASQLTTR RIEDVRLRLL QMFNADPAEF DVVFVANATA GIKLVAEAFR DQDGGFWYGY
     HRDAHTSLIG VREVAATHRC FTTDGEVNAW IDSDENGSGS TQLFAYPAQS NMNGRRLPLG
     WSRRIRANKQ NAVYTLLDAA ALVSTSPLNL GNPDEAPDFT VLSLYKIFGF PDLGALIVRQ
     ASASMFDKRR YFGGGTVDMV VCLKEQWHAK KADSLHERLE DGTLPIHSIM ALDSAMTVHQ
     ELYTSLERVS WHTTFLVQRL YEGLLSLRHG NGHEVCHVYK DPASTYGDSL TQGPIVAFNL
     CNPFGGWVSN AEVEKLAAIK NIHLRTGGLC NPGGVASSLG LAPWEMRDNF SAGQRCGNDN
     DIIHAKPTGI IRVSVGAMST LSDVEYFVAF VREFFVQDSP PLDASPMTVV EVEPPTQSRL
     HVESLSVYPI KSCAGFSVPP GTAWEVRPEG LVWDREWCLV HQGTGAALSQ KRYPKMALIR
     PSIDVEKGVL RVKLAGVLQE TTTTHEITVP LSADPRLFAE DAMYKDASAK VCGDAIKAKT
     YRSSDISDFF TQALGVACHL ARFPAVGNGS GVSRHSKAHL QKYPKTGAMR VPGAFPETAA
     MMAGACVSKP ILLANESPIL TISRASLNRL NEMIKAEGGK AAQAEVFRAN IVVAEHPAYP
     PGLEEPYAED EWRYVQIGQQ FFEMLGGCRR CQMVCIDQQT GERNQEPFVT LSKTRRFEGR
     VYFGEHTCHV SSLSTQNPTI TVGDAVRPIR DGEVDENSVL RALVG
//
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