ID A0A0J5LTV7_PLUGE Unreviewed; 804 AA.
AC A0A0J5LTV7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:KMK11415.1};
GN ORFNames=ABW06_21260 {ECO:0000313|EMBL:KMK11415.1};
OS Pluralibacter gergoviae (Enterobacter gergoviae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Pluralibacter.
OX NCBI_TaxID=61647 {ECO:0000313|EMBL:KMK11415.1, ECO:0000313|Proteomes:UP000036196};
RN [1] {ECO:0000313|EMBL:KMK11415.1, ECO:0000313|Proteomes:UP000036196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS81F13 {ECO:0000313|EMBL:KMK11415.1,
RC ECO:0000313|Proteomes:UP000036196};
RA Greninger A.L., Miller S.;
RT "Genome sequences of Pluralibacter gergoviae.";
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMK11415.1}.
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DR EMBL; LDZF01000029; KMK11415.1; -; Genomic_DNA.
DR STRING; 61647.LG71_04525; -.
DR PATRIC; fig|61647.14.peg.2520; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR Proteomes; UP000036196; Unassembled WGS sequence.
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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000036196}.
SQ SEQUENCE 804 AA; 89591 MW; FA542AC312697F69 CRC64;
MTNHWVDIKN ANLVVVMGGN AAEAHPVGFR WAMEAKIHNG AKLIVIDPRF TRTASVADFY
TPIRSGTDIT FLSGVMLYLL TNEKINREYT EAYTNASLIV REDYAFEDGL FSGYDADKRK
YDKTSWNYEL DENGHAKRDT TLTHPRCVWN LLKQHVSRYT PEVVEKICGT PKADFLKVCE
YIAETSAPDK TASFLYALGW TQHSVGAQNI RTMAMIQLLL GNMGMAGGGV NALRGHSNIQ
GLTDLGLLSQ SLPGYLNLPS EKQTDLQTYL TASTPKPLLE GQVNYWGNYP KFFVSMMKAF
FGDKATKENN WGFDWLPKWD KSYDVLQYFE MMYKGEVNGY ICQGFNPVAS FPNKNKIVAS
LSKLKFLVTI DPLNTETSTF WQNHGESNDV DPAKIQTEVF RLPSTCFAEE NGSIVNSGRW
LQWHWKGADA PGIARTDGEI LAGIFLRLRE MYAKEGGPVP EPVLNMTWNY TTPDEPASEE
VAMESNGKAL ADITDPATGA VIVKKGQQLT SFAQLRDDGS TSSGCWIFTG SWTPEGNQMA
RRDNADPSGL GNTLGWAWAW PLNRRILYNR ASADPQGKPW DPKRQLLKWD GAKWGGVDIP
DYSAAAPGSD VGPFIMQPEG MGRLFAIDKM AEGPFPEHYE PFETPLGTNP LHPNVVSNPA
ARVFKDDLDA MGKADKFPYV GTTYRLTEHF HYWTKHALLN AIAQPEQFVE IGEKLANKLG
ITHGDTVKVS SNRGYIKAKA VVTKRIRTLK VNDKDVDTIG IPIHWGYEGV AKKGFIANTL
TPFVGDANTQ TPEFKTFLVN VEKV
//