ID B2UJH6_RALPJ Unreviewed; 886 AA.
AC B2UJH6;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 105.
DE SubName: Full=Formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:ACD29727.1};
GN OrderedLocusNames=Rpic_4642 {ECO:0000313|EMBL:ACD29727.1};
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29727.1};
RN [1] {ECO:0000313|EMBL:ACD29727.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=12J {ECO:0000313|EMBL:ACD29727.1};
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; ACD29727.1; -; Genomic_DNA.
DR AlphaFoldDB; B2UJH6; -.
DR STRING; 402626.Rpic_4642; -.
DR KEGG; rpi:Rpic_4642; -.
DR PATRIC; fig|402626.5.peg.886; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_0_4; -.
DR OMA; TKYCAVK; -.
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: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 InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 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; 2.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 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};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..78
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 133..162
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 176..205
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; 95264 MW; DC7E9DD32A9A4876 CRC64;
MVRLTIDGAP WETAEGTLLI DALSAAGSAV PNLCHDKRLM PFGGCRLCVV HVDGYANPVA
SCTTEVAEGM SVQTDSSTLQ ALCRTNLELI AARYPRSAYA ADPRHPFHRL LTDYGVPPGG
KREDGLFRDD SHPYLGVSMD RCVYCQRCVR ICEEVQGQFI WEAIGRNDAS RIAVGRGPTL
REAGCVSCGA CVDTCASGAL FDKRQVSRPT AWTRTTCAYC GVGCQMDVGV ANGRVVTVRP
ADRPVNRGHL CVKGRYAFEY NHAPDRVTQP MLRRDGRWQP VGWGEALDFA ATQLQAIVMR
HGPDAVGVLA SSRATNEENY LAQKFARVVL GTHNIDCCAR VCHTPSARAL QTMLGIGAAT
NSFDDIERAS AFLVCGANPT ENHPVVGARI KQAVLKGARL VVIDPRRTEL AALADVHLPV
RTGCNVPLFN ALAAAMIEEG WVDRAFLAER VDGFEAFAAH VAAFSPERVA DLCGVPAAAI
RAAARIYAQS RPAMCFHGLG VTEHLQGSEG VMALVNLALL TGNLGKPGAG INPLRGQNNV
QGAAQMGCDP SVLTGAQSIA QAGARFEQAW GTRLPATRGL DVLEMMDAAQ AGRLKALWVM
GYDIYLSLAN ANATAAALAA LDLVIVQDLF VNQTAEAFGT VFLPAASSFE KDGTFMNSDR
RVQRVRAATT APGQARPDWW IIQALAARMG KPKGFAFEGP QQIWDEVRAL WPDGAGLTYA
RLEHEDLHWP CLDQSHPGTA VLHRDAFVGS KTATLVPVPY VPTPEQTDDA YPLLLTTGRV
LDQFNAGTMS CRTPNAALRP SDTLDMAPVD AARLGLVEGE MVRVSSRHGS AALPLHITDA
MQAGQLFCSF HRPDLRINAL TSPVRDWLVH APEFKVTAVR VEKVAG
//