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Database: UniProt
Entry: A4TV58_9PROT
LinkDB: A4TV58_9PROT
Original site: A4TV58_9PROT 
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
//
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