ID A4TV58_9PROT Unreviewed; 928 AA.
AC A4TV58;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE SubName: Full=Formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:CAM74515.1};
DE EC=1.2.1.2 {ECO:0000313|EMBL:CAM74515.1};
GN Name=fdhA {ECO:0000313|EMBL:CAM74515.1};
GN ORFNames=MGR_1923 {ECO:0000313|EMBL:CAM74515.1};
OS Magnetospirillum gryphiswaldense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=55518 {ECO:0000313|EMBL:CAM74515.1};
RN [1] {ECO:0000313|EMBL:CAM74515.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MSR-1 {ECO:0000313|EMBL:CAM74515.1};
RX PubMed=17449609; DOI=10.1128/JB.00119-07;
RA Richter M., Kube M., Bazylinski D.A., Lombardot T., Gloeckner F.O.,
RA Reinhardt R., Schueler D.;
RT "Comparative genome analysis of four magnetotactic bacteria reveals a
RT complex set of group-specific genes implicated in magnetosome
RT biomineralization and function.";
RL J. Bacteriol. 189:4899-4910(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; CU459003; CAM74515.1; -; Genomic_DNA.
DR AlphaFoldDB; A4TV58; -.
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; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
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; 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:CAM74515.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 17..95
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 95..134
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 157..188
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 200..229
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 236..292
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 928 AA; 100244 MW; 739F9CC8081CA336 CRC64;
MTLRSKDFGT PARSDAALVS VTIDGHTISV PAGTSVMRAA AQAGIMIPKL CATDHLEAFG
SCRLCLVEIS GRKGTPASCT TPVAEGMSVC TNNPRLAALR KGVMELYISD HPLDCLTCPA
NGDCELQDMA GAVGLRQVRY GFAGDNHLAE AKDSSNPYFQ YDPAKCIVCS RCVRACAEVQ
GTFALNVAGR GFDSRIRPGA APDFMGSECV SCGACVQACP TATLIEKSVV RLGQPEHAVE
TTCAYCGVGC SFRAEMQGDT VVRMVPSKQG GANEGHSCVK GRFAWGYASH KDRQLQPMIR
ERITDPWQVV GWDEAIAHTA RRFREVQERH GPRSIGGITS SRCTNEEIYA VQKMIRAGFG
NNNVDTCARV CHSPTGYGLK QTYGTSAGTQ DFKSVDKADV IIVMGANPTA GHPVFASRLK
RRVRQGAKLV VIDPRAIDLV KSPHVSADYH LQLQPGTNVA MVNALAHVVV TEGLVKTDFV
AQRCDLANFR EWADFVGQDR HSPEALESVT GVPAALVRQA ARLYATGGNA AIYYGLGVTE
HSQGSTTVMG IANLAMATGN VGRDGVGVNP LRGQNNVQGS CDMGSFPHEF SGYREVKDDA
VRALFEVVWG RELDAEPGLR IPNMFDQALH GQYKGMFVHG EDIAQSDPNT NHVTAALESL
DFLVVQDLFL NETAAYAHVF LPGTSFLEKD GTFTNAERRI NRVRPAMAPR TGWHEWQVAA
AIATAMGYPM HWQSGADIMA EIARVTPSFK GVSFDRLDKV GSLQWPVTDQ APDGTPIMHV
DGFVRGKGNF VLTEFVPTTE QTSRFFPLIL TTGRILSQYN VGAQTRRTDN VAWHPEDVLE
IHPHDAELRG IACGDMVSLA SRMGATSLRA EITERVPQGV VYTTFHHPVT GANVVTTDNS
DWATNCPEYK VTAVQVSIAN AVHTLVAE
//