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Database: UniProt
Entry: B2UJH6_RALPJ
LinkDB: B2UJH6_RALPJ
Original site: B2UJH6_RALPJ 
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
//
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