ID W8TXQ3_ECOLX Unreviewed; 804 AA.
AC W8TXQ3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Formate dehydrogenase-N subunit alpha {ECO:0000313|EMBL:RDA38600.1};
GN Name=fdnG {ECO:0000313|EMBL:RDA38600.1};
GN ORFNames=A9X72_24445 {ECO:0000313|EMBL:AVU68125.1}, CIG67_13730
GN {ECO:0000313|EMBL:RVE12385.1}, CR538_24740
GN {ECO:0000313|EMBL:AUK03351.1}, DTL43_12720
GN {ECO:0000313|EMBL:RDA38600.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:RDA38600.1, ECO:0000313|Proteomes:UP000253687};
RN [1] {ECO:0000313|EMBL:AVU68125.1, ECO:0000313|Proteomes:UP000325046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=190 {ECO:0000313|EMBL:AVU68125.1,
RC ECO:0000313|Proteomes:UP000325046};
RA Hoffmann M., Sanchez M., Timme R., Bry L.;
RT "Whole genome sequencing of cultured foodborne pathogen.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RVE12385.1, ECO:0000313|Proteomes:UP000288459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCPM 6219 {ECO:0000313|EMBL:RVE12385.1,
RC ECO:0000313|Proteomes:UP000288459};
RA Liu S.-L., Zhou Y.-J., Zhao M.-F.;
RT "Sequencing of Escherichia coli CCPM 6219.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AUK03351.1, ECO:0000313|Proteomes:UP000234238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14EC029 {ECO:0000313|EMBL:AUK03351.1,
RC ECO:0000313|Proteomes:UP000234238};
RA Li B., Wang X.;
RT "mcr-1 positive E.coli isolates in China.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:RDA38600.1, ECO:0000313|Proteomes:UP000253687}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AVC211 {ECO:0000313|EMBL:RDA38600.1,
RC ECO:0000313|Proteomes:UP000253687};
RA Cummins M.L., Reid C.J., Roy Chowdhury P., Bushell R., Esbert N.,
RA Tivendale K.A., Noormohammadi A.H., Islam S., Marenda M.S., Browning G.F.,
RA Markham P.F., Djordjevic S.P.;
RT "Whole Genome Sequence Analysis of Avian Pathogenic E. coli - An Australian
RT Perspective.";
RL Submitted (JUL-2018) 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; CP024141; AUK03351.1; -; Genomic_DNA.
DR EMBL; CP020520; AVU68125.1; -; Genomic_DNA.
DR EMBL; QOGZ01000012; RDA38600.1; -; Genomic_DNA.
DR EMBL; NPIM01000136; RVE12385.1; -; Genomic_DNA.
DR RefSeq; WP_000181540.1; NZ_JAJPBP010000040.1.
DR Proteomes; UP000234238; Chromosome.
DR Proteomes; UP000253687; Unassembled WGS sequence.
DR Proteomes; UP000288459; Unassembled WGS sequence.
DR Proteomes; UP000325046; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0047111; F:formate dehydrogenase (cytochrome-c-553) activity; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0036397; F:formate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IEA:InterPro.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006443; Formate-DH-alph_fdnG.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR NCBIfam; TIGR01553; formate-DH-alph; 1.
DR PANTHER; PTHR43598:SF6; FORMATE DEHYDROGENASE-O 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.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_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}.
FT DOMAIN 2..377
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 682..797
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 804 AA; 89528 MW; D4C17BFB806F3218 CRC64;
MTNHWVDIKN ANLVVVMGGN AAEAHPVGFR WAMEAKIHNG AKLIVIDPRF TRTAAVADYY
APIRSGTDIA FLSGVLLYLL NNEKFNREYT EAYTNASLIV REDYGFEDGL FTGYDAEKRK
YDKSSWTYEL DENGFAKRDT TLQHPRCVWN LLKQHVSRYT PDVVENICGT PKDAFLKVCE
YIAETSAHDK TASFLYALGW TQHSVGAQNI RTMAMIQLLL GNMGMAGGGV NALRGHSNIQ
GLTDLGLLSQ SLPGYMTLPS EKQTDLQTYL TANTPKPLLE GQVNYWGNYP KFFVSMMKAF
FGDKATAENS WGFDWLPKWD KGYDVLQYFE MMKEGKVNGY ICQGFNPVAS FPNKNKVIGC
LSKLKFLVTI DPLNTETSNF WQNHGELNEV DSSKIQTEVF RLPSTCFAEE NGSIVNSGRW
LQWHWKGADA PGIALTDGEI LSGIFLRLRK MYAEQGGANP DQVLNMTWNY AIPHEPSSEE
VAMESNGKAL ADITDPATGA VIVKKGQQLS SFAQLRDDGT TSCGCWIFAG SWTPEGNQMA
RRDNADPSGL GNTLGWAWAW PLNRRILYNR ASADPQGNPW DPKRQLLKWD GTKWTGWDIP
DYSAAPPGSG VGPFIMQQEG MGRLFALDKM AEGPFPEHYE PFETPLGTNP LHPNVISNPA
ARIFKDDAEA LGKADKFPYV GTTYRLTEHF HYWTKHALLN AILQPEQFVE IGESLANKLG
IAQGDTVKVS SNRGYIKAKA VVTKRIRTLK ANGKDIDTIG IPIHWGYEGV AKKGFIANTL
TPFVGDANTQ TPEFKSFLVN VEKV
//
