ID L5N5Y6_9BACI Unreviewed; 979 AA.
AC L5N5Y6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=D479_12523 {ECO:0000313|EMBL:ELK46066.1};
OS Halobacillus sp. BAB-2008.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=1246484 {ECO:0000313|EMBL:ELK46066.1, ECO:0000313|Proteomes:UP000010769};
RN [1] {ECO:0000313|EMBL:ELK46066.1, ECO:0000313|Proteomes:UP000010769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-2008 {ECO:0000313|EMBL:ELK46066.1,
RC ECO:0000313|Proteomes:UP000010769};
RX PubMed=23469348;
RA Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Saxena A.K.,
RA Bagatharia S.B.;
RT "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT BAB-2008.";
RL Genome Announc. 1:E00222-12(2013).
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: 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:ELK46066.1}.
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DR EMBL; ANPF01000051; ELK46066.1; -; Genomic_DNA.
DR RefSeq; WP_008637467.1; NZ_ANPF01000051.1.
DR AlphaFoldDB; L5N5Y6; -.
DR PATRIC; fig|1246484.3.peg.2557; -.
DR eggNOG; COG3383; Bacteria.
DR OrthoDB; 9805142at2; -.
DR Proteomes; UP000010769; Unassembled WGS sequence.
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:0015942; P:formate metabolic process; IEA:InterPro.
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:UP000010769}.
FT DOMAIN 3..79
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 79..119
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 139..168
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 182..211
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 258..314
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 936..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 979 AA; 109668 MW; C4ACFCDCF898770A CRC64;
MNEHTVVTIN GTEYLADPEQ NLLDLINTTG EQVPQICYNE SLGPIQTCDT CIVQVNGELT
RACGTEVKAG MKVQTKLPHV HKAQKESLDR ILEKHELYCT VCDYNNGSCE IHNTMADFGL
EHQSRPFQPT SYEKDESGSF YRYDPDQCIL CGRCVEVCQD VQVNETLTID WDRKEPRVIW
DNDVPIDQSS CVNCGQCSTV CPCNAMMEKG MEGEAGFLTD TEPGILKSMI QLTKKVETGY
GPLFAVSDSE AAMREDRIDK TKTVCTYCGV GCSFDVWTKG RQILKVEPNA QSPANGISSC
VKGKFGWDYV NSDERLTKPL VRRGDQFEEV EWEEAIDFIG DRMEKIKAEK GADHLAFISS
SKATNEESYL MQKLARQVIG TNNVDNCSRY CQAPATKGLF RTVGYGGDSG SIDDIAKSKL
VITIGSNTAE SHPVLASRIK RSQKLFDQKL FVFDLRKHEM AKRADRFYRP KAGTDLVWLS
AVTKYILDQG WQDEKFLDQW VNGFEEYRES LEPFTLAYAS DLTGIPVSEL KDVAKEIAES
ESVVICWAMG VTQHMLGSDT STAISNLLLI TGNYGRPGVG AYPLRGHNNV QGCSDFGSMP
DFFPGYEKTT DDEARARYEK AWGVSIPKDP GMDNHEMIES IHAGDLSAMY VMGEDTGVVD
ANINYVTSAF EKLDLFIVQD LFLTKTAEYA DVVLPASPSL EKEGTFTNTE RRIQRLYNSF
DPLEGTKPDW QIIQLIAKRL GYDWNYSHPG EIMAEAAGLA PLFAGVSYDR LEGYQSLQWP
VAEDGSDQPV LFLDGFPFDD KKAKLYPLSY ELMYDTDEQY DLHVNNGRLL EHFHEGNMTY
KSEGIRRKTP NAFIEISPEL AKERGIEEGA EVKLISEAGE ATGVVTVTDR VRGKEIFLPL
NDNGKSAVNY LTDNRVDKDS NTPAYKEIAV KMKVLKKKGK SPIPSNNHRR GDPVPQISVQ
VKKKWQREDY VFPGSQGER
//