ID A0A0N1AIQ2_9PROT Unreviewed; 958 AA.
AC A0A0N1AIQ2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=IP80_02420 {ECO:0000313|EMBL:KPF50820.1};
OS beta proteobacterium AAP65.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1523424 {ECO:0000313|EMBL:KPF50820.1, ECO:0000313|Proteomes:UP000037849};
RN [1] {ECO:0000313|EMBL:KPF50820.1, ECO:0000313|Proteomes:UP000037849}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP65 {ECO:0000313|EMBL:KPF50820.1,
RC ECO:0000313|Proteomes:UP000037849};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:KPF50820.1}.
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DR EMBL; LJHW01000002; KPF50820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1AIQ2; -.
DR STRING; 1523424.IP80_02420; -.
DR PATRIC; fig|1523424.3.peg.1014; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000037849; 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: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; cd02790; MopB_CT_Formate-Dh_H; 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; IPR041925; CT_Formate-Dh_H.
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 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; PF13187; Fer4_9; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 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; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 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:UP000037849}.
FT DOMAIN 15..93
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 150..179
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 193..222
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 229..284
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 958 AA; 101692 MW; 8C0EDB197489B583 CRC64;
MNAFSREADD ALSAPAVPLQ IDGQQVLARP GQTLWALAKE LGIEVPHLCH REGQAPEGNC
RACVVEVQGE RTLAASCCRA ATPGLVVQTA SPRAQSAQRL VLELLLADAP AAQHKADNEL
EAWAQKLGVA GSRFTPKPAA ERPRSETSHP AIAVNLDACI QCTRCVRACR DEQVNEVIGL
AHRGAAAQIV FDMGDALGSS SCVGCGECVQ ACPTGALAPA GGVALQAADQ VVDSLCPYCG
VGCQVSYHVK DDQILHVEGR SGPANEGRLC VKGRYGFDYA RHPQRLTVPL IRRADAPKDP
HAATDPATAR TQFREASWEE ALALAGGTLR QLREAHGPRA LAGFGSAKGS NEEAYLFQKL
VRLGFGSNNV DHCTRLCHAS SVAALLEGIG SGAVSNPVMD VMQAEVVIVI GANPVVNHPV
AATWIKNAAR QGTQLVVMDP RRSELCRHAA HHLAFRPDTD VALLNSLMYV IVEEGLTDAR
FIAERTEGYA AFAENLRGFS PETMAAVTGI AAETVRTVAR LYAQSRGSMI LWGMGVSQHV
HGTDNARCLI ALALMTGQIG RPGTGLHPLR GQNNVQGASD AGLIPMMYPD YHPVGDPAAR
AAAAALWGVA PETLDADKGL TVVEVMQAAA AGRLKGLYVM GENPAMSDPD ATHAREAMAK
LDMLVVQDLF LTETACLADV VLPASAFAEK TGSFTNTDRL VQLGRRALGL PGQARQDLWI
LTAMAEQLGL DWHGYGATPS DCDAAAGRVF DEMRQLMPTL QGLSWARLQH EGAVTYPCTD
AQAPGERVVF TEHFPRPGGK ALFVPAQLIP ADERPDADYP HVLITGRQLE HWHTGSMTRR
SGVLDALEPD PVVLLHPQEL AALGVAPGGL VTLQSRRGEV SLYARADEGT PPGAVFVAFC
WFEAAINRLT NPALDPVAKI PEFKYCAVRL RAGGVAPGQG SFGGGQRWRE QAGAAMPG
//
