ID A0A0G3HCW7_9CORY Unreviewed; 599 AA.
AC A0A0G3HCW7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Molybdopterin dinucleotide binding protein {ECO:0000313|EMBL:AKK10565.1};
GN ORFNames=CUTER_02755 {ECO:0000313|EMBL:AKK10565.1};
OS Corynebacterium uterequi.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1072256 {ECO:0000313|EMBL:AKK10565.1, ECO:0000313|Proteomes:UP000035548};
RN [1] {ECO:0000313|EMBL:AKK10565.1, ECO:0000313|Proteomes:UP000035548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45634 {ECO:0000313|EMBL:AKK10565.1,
RC ECO:0000313|Proteomes:UP000035548};
RX PubMed=26227590;
RA Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.;
RT "Virulence Factor Genes Detected in the Complete Genome Sequence of
RT Corynebacterium uterequi DSM 45634, Isolated from the Uterus of a Maiden
RT Mare.";
RL Genome Announc. 3:e00783-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000035548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45634 {ECO:0000313|Proteomes:UP000035548};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium uterequi DSM 45634, isolated
RT from the uterus of a maiden mare.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP011546; AKK10565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3HCW7; -.
DR STRING; 1072256.CUTER_02755; -.
DR KEGG; cut:CUTER_02755; -.
DR PATRIC; fig|1072256.5.peg.545; -.
DR Proteomes; UP000035548; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00022485};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000035548}.
FT DOMAIN 116..160
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 407..528
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
FT REGION 568..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 599 AA; 65913 MW; C9A96A04303EEF74 CRC64;
MARAFNTSLL KAYFGDAATK DNDFGYHWLP RIDGKHGTYQ TMMNMADGLV EGYLVFGQNP
AVSSINGKLH RKAFRTAKWM VVRDKEMIET ANFWRNSPEH ETGEVTAEDI GTEVFYLPAA
AHVEKAGSFT QTQRMVQFRE KAVEPPGDAQ SELDFFFQLG QRLRERLAGS TDPRDRALLN
MTWDYASAAD PLRADPEAVL GEINGYYLTG ERAGQPLDKF VDMKDDGSTS GGCWIYAGVY
AGGVNHAAKR TPAKSPTDPA PDWGWIWPAN RRVLYNRASA DPQGRPWSER KKYVWWDEAA
GQWTSTGDVV DFPATLRPDF VADPAAQGAG ALCGTDAFIM QDDGKAWLFA PSGVVDGPLP
AHYEAQESRV ANPLYNVQSS PSRGLYSRSD NLQTPPVGSD GSQVYPFTFT TYRVTEQHGA
GGKSRWVPYL AELQPEQFCE VSPELAELRR LEHGGWATII TPRSAIEARV LVTERMKART
VDGRQFHQIG LPFHFANYGE GAEVTGDSAN DLIGVTLEPN ASIQQAKVTA CDIQPGRRPR
GRALTQFVAA YRERAGITAE TGMDRVLVPG EPERDFDPTG VQGGPCAEDD TTAEKPQGA
//
