ID Q0BQS0_GRABC Unreviewed; 986 AA.
AC Q0BQS0;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=NAD-dependent formate dehydrogenase alpha subunit (FdsA) {ECO:0000313|EMBL:ABI62832.2};
DE EC=1.2.1.2 {ECO:0000313|EMBL:ABI62832.2};
GN OrderedLocusNames=GbCGDNIH1_1934 {ECO:0000313|EMBL:ABI62832.2};
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165 {ECO:0000313|EMBL:ABI62832.2, ECO:0000313|Proteomes:UP000001963};
RN [1] {ECO:0000313|EMBL:ABI62832.2, ECO:0000313|Proteomes:UP000001963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1 {ECO:0000313|Proteomes:UP000001963};
RX PubMed=17827295; DOI=10.1128/JB.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J.III., Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005404}.
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; CP000394; ABI62832.2; -; Genomic_DNA.
DR AlphaFoldDB; Q0BQS0; -.
DR STRING; 391165.GbCGDNIH1_1934; -.
DR KEGG; gbe:GbCGDNIH1_1934; -.
DR eggNOG; COG3383; Bacteria.
DR Proteomes; UP000001963; Chromosome.
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 InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
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; PF12838; Fer4_7; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 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; PS51839; 4FE4S_HC3; 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};
KW Oxidoreductase {ECO:0000313|EMBL:ABI62832.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001963}.
FT DOMAIN 57..135
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 135..174
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 197..228
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 241..270
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 277..333
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 986 AA; 108550 MW; F05FAB5E29D8182B CRC64;
MRAGRLHPLS GGQRDDPFPR GFRSPHRPGG SGISERRPPM PLVEEIDYGT PKVVSEKSVT
LTIDGRQVTV PEGTSLMRAA MDTGITVPKL CASDNLKAFG SCRLCLVEIE GRPGTPASCT
TPAMEGMVVH TQTDRLARLR KGVMELYISD HPLDCLTCSA NGDCELQDMA GAVGLREVRY
GYEGENHLHD SKDVSNPYFQ YDPSKCIVCN RCVRACEEVQ GTFALTIEGR GFESRVSPGA
AHDNFFSSEC VSCGACVQAC PTATLMEKSV IEIGQPEHSE VTTCAYCGVG CSFKAEMRGE
QIVRMVPYKD GKANHGHSCV KGRFAYGYAL HKDRQLEPMI REKITDPWRV VSWDEAIQYT
AKEFRRIQDK YGRSSIGGIT SSRCTNEETY LVQKLVRAVF GNNNVDTCAR VCHSPTGYGL
KTTYGTSAGT QDFDSVEESD VIVVIGANPV DAHPVFGSQM KRRLRDGAKL IVIDPRKTDL
VKSPHIKADF HLPLRPGTNV AIVSALAHVV VTEGLLDEAF VRERTDWESF QDWVQFVTRP
ENSPEAVAEI CGVSAEDIRG AARLYATGGN AAIYYGLGVT EHSQGTTTVM AIANLAMATG
NLGRRGVGVN PLRGQNNVQG SCDMGSFPHE FTDYRHVSND AARAQFEALW GVSLDAEPGL
RIPNMIDAAV DGTYKGIYIQ GEDIVQSDPD TTHMIAGLKN MECVVVQDLF LNETADYAHV
FLPGCSFLEK DGTFTNAERR INRVRKVMSP KNGYGDWEIT QMLAKAMGYP MHYNHPSEIM
DEIAATTPNF ALVSYAKLDE AGSVQWPCND EHPDGMPIMH IGQFSRGKGY FVVTEYIATD
EKTGPLFPLL LTTGRILSQY NVGAQTRRTH NSMWHEEDRL DIHPKDAEDR GVRDGDWVKL
ESRSGATSLR ARITEKVPPG VVYTTFHHPA SQANVVTTDN SDWATNCPEY KVTAVQVQRS
NGPTEWQREY GDHSTQARRI IPAAAE
//
