ID D8JSG9_HYPDA Unreviewed; 965 AA.
AC D8JSG9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:ADJ24263.1};
GN OrderedLocusNames=Hden_2466 {ECO:0000313|EMBL:ADJ24263.1};
OS Hyphomicrobium denitrificans (strain ATCC 51888 / DSM 1869 / NCIMB 11706 /
OS TK 0415).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=582899 {ECO:0000313|EMBL:ADJ24263.1, ECO:0000313|Proteomes:UP000002033};
RN [1] {ECO:0000313|Proteomes:UP000002033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51888 / DSM 1869 / NCIB 11706 / TK 0415
RC {ECO:0000313|Proteomes:UP000002033};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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; CP002083; ADJ24263.1; -; Genomic_DNA.
DR RefSeq; WP_013216422.1; NC_014313.1.
DR AlphaFoldDB; D8JSG9; -.
DR STRING; 582899.Hden_2466; -.
DR KEGG; hdn:Hden_2466; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_0_5; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000002033; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002033}.
FT DOMAIN 21..99
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 99..138
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 173..204
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 216..245
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 252..308
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 965 AA; 106683 MW; A56CD33E73B2B374 CRC64;
MTLIKETDYG TKTPEVHETT KMVTLEIDGF EVTVPEGTSI MNAAMQLGIQ IPKLCATDSL
DPFGSCRLCL CEIEGRRGTP ASCTTPVAQG IKVATQNQRL AKLRRGVMEL YISDHPLDCL
TCAANGDCEL QDMAGAVGLR EVRYGYDGEN HVFAKRADGS ANDRFKQTDV SNPYFQFQPS
KCIVCSRCVR ACEEVQGTFA LTIDGRGFAS HVSAGMDEQF LASECVSCGA CVQACPTATL
IEKSVVDMGQ PEHSIITTCA YCGVGCSFKA EMRGDELVRM VPYKDGGANE GHSCVKGRFA
FSYATHKDRM LTPMIREKIT DPWQVVTFDE AINYAAKRFM ETQAKYGRKS IGAVTSSRTT
LEEIYSVQKL VRGAFNNNNV DTCARVCHSP TGFGLKVAFG EAAGTQDFKS TDKTDVMLVI
GCNPTDAHPV FGSRMKKRIR EGAKLIVIDP RKVELVDSPH VKADYHLQLM PGTNVAVANA
IGHVIATENL IDRKFVNRRC EKTDFHRWEE FIRQPQHAPE AVEHITRVPA QLIREAARLY
ATGGNAAIYY GLGVTEHTQG STTVMALANL AMATGNLGRE GVGVNPLRGQ NNVQGSSDMG
SAPHEFPGYR HVSNQEVRDI YKKEWNRELD PEPGLRIPNM FDAALDGSYR GMFIHGEDIA
QSDPDTHHVE AALRAMDIVV VQDLFLNETA AFAHVFLPGT SFLEKDGTFV NAERRVNRVR
KVFQEKQGMP EWAIVAQLAT AMGFPMYYAT ASEVMDEIAR TTPTFSGISY DRLDELGSIQ
WPCNDQHPTG TPIMHTEEFV RGKGRFMLTA YMATDEKASN TFPLILTTGR ILSHYNVGAQ
TRRTDNMAWH PEDVLEMHPY DAEIRGLKDD QIVSLTSRAG ATTIRVKISD RMPQGVVYTT
FHHPGTGANL ITTSASDWAT NCPEYKVTAV QVMPSNQPSD WQSEWNIRNV ESKRISTEKK
LEPAE
//
