ID A0A3S0QVZ5_9BACI Unreviewed; 974 AA.
AC A0A3S0QVZ5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:RTQ93436.1};
GN ORFNames=EKG35_08555 {ECO:0000313|EMBL:RTQ93436.1};
OS Lysinibacillus telephonicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1714840 {ECO:0000313|EMBL:RTQ93436.1, ECO:0000313|Proteomes:UP000276349};
RN [1] {ECO:0000313|EMBL:RTQ93436.1, ECO:0000313|Proteomes:UP000276349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S5H2222 {ECO:0000313|EMBL:RTQ93436.1,
RC ECO:0000313|Proteomes:UP000276349};
RA Yu L.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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:RTQ93436.1}.
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DR EMBL; RXNR01000019; RTQ93436.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0QVZ5; -.
DR OrthoDB; 9805142at2; -.
DR Proteomes; UP000276349; 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: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:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-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; IPR027467; MopterinOxRdtase_cofactor_BS.
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; PS00551; MOLYBDOPTERIN_PROK_1; 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:UP000276349};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..76
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 76..116
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 138..165
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 181..210
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 257..312
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 936..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 974 AA; 108353 MW; 307192F1312D983A CRC64;
MTKININGVS YELTEGATIL DIINQNGIEH PQICHVPSVD PIQTCDTCIV EVDGQLVRSC
STKALDGMNI QLQSDKAKAA QTEAMDRLLE NHMLYCTVCD NNNGNCTLHN TVEMMEIEHQ
KYPFKPKVEP HEVDMTHPFY RYDPNQCIAC GQCVEVCQNL QVNETLSIDW EAERPRVIWD
DGVNINDSSC VSCGQCVTVC PCNALMEKSM LGEAGFMTGL KQDTLDPMID LIKEVEPGYS
GIFAISEVEA AMRSKRTKKT KTVCTFCGVG CSFEVWTKDR KILKVQPSDG PVNAVSTCIK
GKFGWDFVNS EERITKPLIR KNEEFVESTW DEALDLIASK LGGIQKEFGP GSVGFISSSK
ITNEENYLIQ KMARQLFGTN DVDNCSRYCQ SPATDGLLRT VGFGGDAGTI KDIAKAGLVI
IVGANPTEGH PVLATRVKRA HKLHGQKLIV ADVRKHEMAE RSDIFMRPKQ GTDQVWLMAV
TKYIIDQGWH DEAFIKENVH DFGAFKFVLE KYTLDYAEEV TGISKETLIN VAEMIRDADG
TCVLWGMGVT QNTGGSYTSA AISNLLLATG NYRRPGAGAY PLRGHNNVQG ACDMGTLPNL
LPGYQKVTDD EARAKFEKAY GVKIQPKPGR NNPQMLDAIM EGKMKAMYLV GEDMALVDAD
ANHVDKVLSS LDFFVVQDVF LSRTAQYADV VLPAAPSLEK EGTFTNTERR VQRLYQVLPT
LGESKADWEI LQLVANRLGA EWNYSHPSEI FDEMASLSPI FSQANYDVLE GWGSFNWGSH
DGKDTPLLYE DGFNFPDKKA RFALDDWMKP VEYEPEYDCH INNGRMLEHF HEGNMTNKSK
GIQSKVPEIF VEVSPEMAKE RGIEDGTLLR LVSPYGALKL NALVTDRVQG NELFLPMNST
SKDSAINFLT GGGADVNTST PAYKQTKVRV EVLKAKGKSP LPRTNPRNKK RHPQNGVEVQ
RKWNRPGYVH LTTN
//
