ID A0A2I6SA17_9RHOO Unreviewed; 951 AA.
AC A0A2I6SA17;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=C0099_14830 {ECO:0000313|EMBL:AUN96100.1};
OS Pseudazoarcus pumilus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Pseudazoarcus.
OX NCBI_TaxID=2067960 {ECO:0000313|EMBL:AUN96100.1, ECO:0000313|Proteomes:UP000242205};
RN [1] {ECO:0000313|EMBL:AUN96100.1, ECO:0000313|Proteomes:UP000242205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY39 {ECO:0000313|EMBL:AUN96100.1,
RC ECO:0000313|Proteomes:UP000242205};
RA Fu G.-Y.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000455};
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; CP025682; AUN96100.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I6SA17; -.
DR KEGG; atw:C0099_14830; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000242205; 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:UniProtKB-EC.
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; IPR006655; Mopterin_OxRdtase_prok_CS.
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; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000242205}.
FT DOMAIN 19..97
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 97..136
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 159..190
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 203..231
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 238..294
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 951 AA; 103841 MW; 56E41A40D0A119B0 CRC64;
MLYQLNDIDY GTPASVSENL VTLTIDGVAV TVPEGTSVMR AAVEAGINIP KLCATDSLEA
YGSCRLCVVE IEGRRGTPAS CTTPVDEGMI VNTQTGKLAD LRRNVMELYI SDHPLDCLTC
SANGNCELQD MAGVVGLREV RYGYEGENHL SDTTDYSNPY FNYDPSKCIV CNRCVRACEE
TQGTFALTVD GRGFESRIAA SQNEDFMDSE CVSCGACVQA CPTATLMEKS VVELGQAEHS
VVTTCAYCGV GCSFKAEMKG ETVVRMVPNK NGQANMGHSC VKGRFAWGYA THSDRITKPM
IRKKITDPWQ EVSWEEAIDY AASELKRIQA NYGRGAVGGI TSSRCTNEET YLVQKLVRAA
FGNNNVDTCA RVCHSPTGYG LKVTMGESAG TQTFESVLHS DVIFVIGANP TDGHPVFGSI
MKRRLRAGAK LIVADPRRID LVKSPHVKAD YHLQLRPGSN VALVTSMAHV IVTEGLLNES
FIQERCDLES YEIWKKFVAR EENSPEAMEA VTGVPADVLR GAARLFATGG NAAIYYGLGV
TEHAQGSTTV IGIANLAMAT GNIGRKGVGV NPLRGQNNVQ GACDMGSFPH ELPGYRHVSD
ATARALFEAE WGVSLEGEPG LRIPNMFDAA LEGTYKAMYV QGEDIVQSDP NTQHTTEALE
NLECLIVQDL FLNETAKYAH VFLPGSSFLE KDGTFTNAER RISRVTKVMK PLAGYADWEA
TQLLANALGY PMNYKHPSEI MDEIARLTPT FHGVSFDLID RLGSVQWPCN AEAPEGTPTM
HIDEFVRGKG KFAPTRYVAS DERVTQKFPL ILTTGRILSQ YNVGAQTRRT ANNAWHSEDR
LELHPHDAED RGIKDGDWVG IQSRAGETVL RATITERMQP GVVYTTFHFP ESGANVITTD
SSDWATNCPE YKVTAVQVLP VSQPSEWQQG FARFTEQQLA LLEEARTAGA K
//
