ID J2W464_9BRAD Unreviewed; 957 AA.
AC J2W464;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Formate dehydrogenase, alpha subunit, archaeal-type {ECO:0000313|EMBL:EJN13457.1};
GN ORFNames=PMI42_03196 {ECO:0000313|EMBL:EJN13457.1};
OS Bradyrhizobium sp. YR681.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1144344 {ECO:0000313|EMBL:EJN13457.1, ECO:0000313|Proteomes:UP000007272};
RN [1] {ECO:0000313|EMBL:EJN13457.1, ECO:0000313|Proteomes:UP000007272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR681 {ECO:0000313|EMBL:EJN13457.1,
RC ECO:0000313|Proteomes:UP000007272};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJN13457.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKIY01000181; EJN13457.1; -; Genomic_DNA.
DR RefSeq; WP_008135071.1; NZ_AKIY01000181.1.
DR AlphaFoldDB; J2W464; -.
DR PATRIC; fig|1144344.3.peg.2780; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000007272; 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"
SQ SEQUENCE 957 AA; 104598 MW; 9C1C527D52C509C2 CRC64;
MSLIEEIDYG TPRSKSTTMV TLTIDGNEVT VPEGTSIMRA AMDAGHQIPK LCATDMVDAF
GSCRLCVVEI EGRAGTPASC TTPVMPGLVV HTQSERLKKL RKGVMELYIS DHPLDCLTCG
ANGDCELQDM AGAVGLRDVR YGYEGENHVF AKSHGEINAA WMPKDESNPY FTYDPSKCIV
CSRCVRACEE VQGTFALTIS GRGFDSRVSP GMSESFLGSE CVSCGACVQA CPTATLTEKS
VIEIGQPEHS VVTTCAYCGV GCAFKAEMRG EEVVRMVPYK DGKANRGHSC VKGRFAWGYT
NHKERILNPM IRERIEDPWK EVSWDEAFSF AAAKMRGIQK KYGRDAIGGI TSSRCTNEET
YLVQKLIRGG FGNNNVDTCA RVCHSPTGYG LSQTFGTSAG TQDFDSVEDT DVAVIIGANP
ASAHPVFASR LKKRLRQGAK LIVIDPRRTE MVESPHVKAL HLPLMPGTNV AVVTALAHVI
VTEGLANEAF VRERCDWAEF EEWAAFVAQP KHSPEATAIL TGVDPNDLRE AARIYATGGN
GAIYYGLGVT EHSQGSTTVI AIANLAMATG NIGRPGVGVN PLRGQNNVQG SCDMGSFPHE
LPGYRHISGD AVRDQFEALW NVKLNPEPGL RIPNMFDAAI EGTFMGIYVQ GEDILQSDPN
TKHVVAALSA MECVIVHDLF LNETANYAHV FLPGSSFLEK DGTFTNAERR IQRVRKVMSP
KNGMADWEVT IALAKAMGFE MNYNHPSEIM DEIAALTPTF TGVSYAKLDE LGSVQWPCNE
KAPEGTPVMH IGGFVRGKGK FIVTEYVATD ERTGPRFPLL LTTGRILSQY NVGAQTRRTE
NVVWHAEDRL EIHPHDAEQR GVRDGDWVRL QSRAGETTLR AEITDRVSPG VVYTTFHHPD
TQANVITTDY SDWATNCPEY KVTAVQISPS NGPSDWQKAY DEQARHSRRI VPAEAAE
//
