ID A0A0R3MFP8_9BRAD Unreviewed; 957 AA.
AC A0A0R3MFP8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:KRR18907.1};
GN ORFNames=CQ14_18600 {ECO:0000313|EMBL:KRR18907.1};
OS Bradyrhizobium lablabi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=722472 {ECO:0000313|EMBL:KRR18907.1, ECO:0000313|Proteomes:UP000051660};
RN [1] {ECO:0000313|EMBL:KRR18907.1, ECO:0000313|Proteomes:UP000051660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCBAU 23086 {ECO:0000313|EMBL:KRR18907.1,
RC ECO:0000313|Proteomes:UP000051660};
RA Duran D., Rey L., Navarro A., Busquets A., Imperial J., Ruiz-Argueso T.;
RT "Bradyrhizobium valentinum sp. nov., isolated from effective nodules of
RT Lupinus mariae-josephae, a lupine endemic of basic-lime soils in Eastern
RT Spain.";
RL Submitted (MAR-2014) 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=[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}.
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:KRR18907.1}.
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DR EMBL; LLYB01000101; KRR18907.1; -; Genomic_DNA.
DR RefSeq; WP_057861244.1; NZ_LLYB01000101.1.
DR AlphaFoldDB; A0A0R3MFP8; -.
DR STRING; 722472.SAMN05444321_4931; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000051660; Unassembled WGS sequence.
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; 2.
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}.
FT DOMAIN 18..96
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 96..135
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 169..200
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 212..241
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 248..304
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 930..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..957
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 104608 MW; 2FA020FF355B2253 CRC64;
MSLIQETDFG TPRSKSETMV TLTIDGQSVT VPEGTSIMRA AMEAGTQIPK LCATDMVDAF
GSCRLCLIEI EGRAGTPASC TTPVMNGLVV HTQTERLKKL RKGVMELYIS DHPLDCLTCA
ANGDCELQDM AGAVGLRDVR YGYEGENHVF AKSDGCTNDN WMPKDESNPY FTYDPSKCIV
CSRCVRACEE VQGTFALTIS GRGFDSRVSP GMSESFLGSE CVSCGACVQA CPTATLTEKS
VIEIGQPEHS VVTTCAYCGV GCAFKAEMRG EEVVRMVPWK DGKANRGHSC VKGRFAWGYT
THKERILKPM IREDIADPWR EVSWDEAFSF AAAKFKGIQA KYGRDAVGGI TSSRCTNEET
YLVQKLIRGG FGNNNVDTCA RVCHSPTGYG LATTFGTSAG TQDFDSVEHT DVVMVIGANP
ASAHPVFASR LKKRLRQGAK LIVVDPRRTE MVEGPHMSAL HLPLMPGTNV AVLTALAHVI
VTEGLVDEAF VRERCDWSEF EEWAAFVALP KNSPESTAIM TGVDPKVLRE AARQFATGGN
GAIYYGLGVT EHSQGSTTVI AIANLAMATG NIGRPGVGVN PLRGQNNVQG SCDMGSFPHE
LPGYRHISGD AVRDQFEAMW NVKLNPEPGL RIPNMFDAAI EGTFMGIYVQ GEDILQSDPN
TKHVVAALSS MECVIVHDLF LNETANYAHV FLPGSTFLEK DGTFTNAERR IQRVRKVMTP
RNGLADWEVT IGLAKAMGYD MHYDHPSQIM DEIAALTPTF TGVSYAKLDE LGSVQWPCNE
KAPQGTPVMH IDGFVRGKGK FVITEYVPTD ERTGPRYPLL LTTGRILSQY NVGAQTRRTD
NVVWHSEDRL EIHPHDAEQR GVRDGDWVRL ASRAGETTLR AEITDRVAPG VVYTTFHHPD
TQANVITTDF SDWATNCPEY KVTAVQISPS NGPSDWQKAY DEQARHSRRI APAEAAE
//
