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Database: UniProt
Entry: A0A1Y2VJS6_9PEZI
LinkDB: A0A1Y2VJS6_9PEZI
Original site: A0A1Y2VJS6_9PEZI 
ID   A0A1Y2VJS6_9PEZI        Unreviewed;       825 AA.
AC   A0A1Y2VJS6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=M434DRAFT_391501 {ECO:0000313|EMBL:OTA97892.1};
OS   Hypoxylon sp. CO27-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA97892.1, ECO:0000313|Proteomes:UP000194361};
RN   [1] {ECO:0000313|EMBL:OTA97892.1, ECO:0000313|Proteomes:UP000194361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO27-5 {ECO:0000313|EMBL:OTA97892.1,
RC   ECO:0000313|Proteomes:UP000194361};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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:0000256|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:0000256|HAMAP-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; KZ112422; OTA97892.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2VJS6; -.
DR   STRING; 1001938.A0A1Y2VJS6; -.
DR   Proteomes; UP000194361; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; MOCOS_middle.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR14237; MOLYBDOPTERIN COFACTOR SULFURASE MOSC; 1.
DR   PANTHER; PTHR14237:SF19; MOSC DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   Pfam; PF03473; MOSC; 1.
DR   Pfam; PF03476; MOSC_N; 1.
DR   SUPFAM; SSF141673; MOSC N-terminal domain-like; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS51340; MOSC; 1.
PE   3: Inferred from homology;
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|HAMAP-Rule:MF_03050};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_03050}; Reference proteome {ECO:0000313|Proteomes:UP000194361};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03050}.
FT   DOMAIN          663..823
FT                   /note="MOSC"
FT                   /evidence="ECO:0000259|PROSITE:PS51340"
FT   ACT_SITE        401
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
FT   MOD_RES         234
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ   SEQUENCE   825 AA;  90903 MW;  5611C8D20817B339 CRC64;
     MTDGGGSTAY NSHIEGLRQN EFPMLRDEVY LDHAGTTLYA RSLVDKFAAD MTSNLFGNPH
     SASLSSQTST SRIEDVRLRV LQFFNADPSE FDLIFVANAT AGIKLVAEAF RCSPLGFNYL
     YHQACHTSLV GVREEAVNSI CLDDTAMGKW LGGDSLSPEI NHHERPVLFA YPAQSNMDGF
     RFPLDWSDKL RKSKSALDFP IFTLLDAAAF VSTSPMDLSK SETAPDFTVL SFYKMFGFPD
     LGGLIVRRQA ASIFRPRKYF GGGTVDMVVC LKEQWHAPKM QALHESLEDG TLPVHSIIAL
     DSALDVHCQL FESMNHVSSH TSFLTQRLHD GLAVLRHSNG QPVCVIYSQP PLASKIPELS
     LGNGPVVAFN LQNHLGGWVS LIEFEKLAVL KRFHIRTGGL CNPGGIARSL GLEPWEMKRN
     FSAGFRCGSD NDIMGGRPTG VIRVSLGAMS TISDVDRFIA FIVEFYRTEN VPICTPSTSA
     PTHQDLPNMC VKSITVFPIK SCGGFRIPAG IMWEVKAEGL AWDREWCLVH RGTGQALSQK
     RHPRMALIQP VIDFSKGQLR VSYRGALSNQ NIPEISVPLS ANPGLFQASA TPKPLASRVC
     GEEISAQIYT SSEVNDFFTT ILGVPCVLAR FPPGGLGKSM RHAKAHLQKH QKVNRKLQYK
     MPCQFPGMDT PPDSDSEAER QRILLSNESP ILMINLSSLE ALNRQIIDRG GNAVSSEVFR
     ANIVVGSSDP DPHSSAYSED HWSSVRIGQQ DFKMLGSCRR CHMVCIDQET AEKSEEPFVT
     LAKTRRFDGK VFFGTHMCHV PAQSGTKEAQ FPTVTVGDEV LIDPV
//
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