ID B2UIT5_RALPJ Unreviewed; 886 AA.
AC B2UIT5;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:ACD29486.1};
GN OrderedLocusNames=Rpic_4391 {ECO:0000313|EMBL:ACD29486.1};
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29486.1};
RN [1] {ECO:0000313|EMBL:ACD29486.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=12J {ECO:0000313|EMBL:ACD29486.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome2 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
CC molybdopterin-containing oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00007023}.
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DR EMBL; CP001069; ACD29486.1; -; Genomic_DNA.
DR AlphaFoldDB; B2UIT5; -.
DR STRING; 402626.Rpic_4391; -.
DR KEGG; rpi:Rpic_4391; -.
DR PATRIC; fig|402626.5.peg.645; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_0_4; -.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:UniProt.
DR GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd00508; MopB_CT_Fdh-Nap-like; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041924; Formate_Dh-H_N.
DR InterPro; IPR006478; Formate_DH_asu.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 1..78
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 176..206
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 210..265
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 886 AA; 95157 MW; 2DDAF44CA6B9B77C CRC64;
MVRLTIDGSP LEVAEGALLI DALSTAGKAV PHVCHDKRLT PSGACRLCLV LVEGQRRPVA
SCTAEVAEGM VVQTRSHALD TLCRTNLELI AARYPRTAYA ADPKHPFHRL LAEYGVPPGG
KHEDGFFTDD SHPYLGVGME RCVHCDRCVR ICEEVQGQFI WETIGRDDTT RIAIGKGPTL
LTAGCVSCGA CVDSCASGAL FDKRSGVKPT AWTRTTCAYC AVGCQMEVGT AGGRVVVVRP
ADSPVNRGHL CLKGRYAFEY NHAPDRVTQP MLRRNGRWQA VGWNEALGFT ASRLQDIIAT
NGADAIGVLG SSRATNEENY LAQKFARVVL GTHNVDCCAR VCHTPSAKAL KTMLGIGAAT
NTFDDIEHAS AFLICGANPT ENHPVVGARI KQAVSRGAQL VVIDPRRTEL AALADVHLPV
RAGSNVLLFN ALAAAIIEEG WVDRTFLSER VIGFDAFAAH VADYAPESVA ERCGVSAPAI
RAAARIYAKG QPAMCFHGLG VTEHLQGSEA VMALINLALL TGNLGRPGSG INPLRGQNNV
QGAAQMGCDP ATLTGAQSIG QAGARFEQVW GAKLPATRGL NVVEMMDAAQ AGRLKALWVM
GYDIYLSLAN ASATAAALGA LDLVIVQDLF INQTAAAFGT VFLPAASAFE KEGTFMNSDR
RVQRVHAVTT APGQARSDWW IIQALAARMG KPEGFEFDGP EQIWDEVRAL WPEGAGLAYS
RLDGENLHWP CPDETHTGTP VLHRERFSGG KTAALIPVAY VPTPERPDDD YPFLLTTGRV
LEHFNAGTMS YRTPNAALRP SDTLDMAPAD AARHGFTEGD VVEVSSRYGS AILPLHISHA
MQIGQLFCSF HRADLLVNRL TSPVRDRLVH TPEYKVTAVR VKKRCN
//
