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
//