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Database: UniProt
Entry: L5N5Y6_9BACI
LinkDB: L5N5Y6_9BACI
Original site: L5N5Y6_9BACI 
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
//
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