ID A0A0S8DL76_9BACT Unreviewed; 897 AA.
AC A0A0S8DL76;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:KPK36928.1};
GN ORFNames=AMJ65_15585 {ECO:0000313|EMBL:KPK36928.1};
OS Phycisphaerae bacterium SG8_4.
OC Bacteria; Planctomycetota; Phycisphaerae.
OX NCBI_TaxID=1703409 {ECO:0000313|EMBL:KPK36928.1, ECO:0000313|Proteomes:UP000051853};
RN [1] {ECO:0000313|EMBL:KPK36928.1, ECO:0000313|Proteomes:UP000051853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_4 {ECO:0000313|EMBL:KPK36928.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK36928.1}.
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DR EMBL; LJTR01000341; KPK36928.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8DL76; -.
DR PATRIC; fig|1703409.3.peg.1843; -.
DR Proteomes; UP000051853; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
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; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_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; PS00641; COMPLEX1_75K_1; 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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..77
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 77..116
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 139..172
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 220..278
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 897 AA; 98443 MW; 688427166F82CC1A CRC64;
MKLTIDGKQI TAQSGQTVLQ AAQDNGIDIP NLCYDPRLKP SGSCRLCLVE IEGQRGLQPS
CVFEARDGLA VKTNTDEIRD IRKTILELLF CEHKARCTVC DENGKCSLQN YAYEYQLSEE
SLGRALGTET GPNYTTANLA LEYDPDKCIR CGRCVRICEE VQMAHALTFK NRAAETEVTT
AFDLPLNEST CVLCGQCIST CPTGALYDRS AIGEGQAKDL VKTRTTCVYC GVGCQIDLNV
NPKKNRIVRV TSEVGCIPND GNLCIKGRFG MDFVGHPERL TTPLIRRDGK LKEATWDEAI
GLIADKLTKI KAESGPDSIA GLSSAKCTNE DNYVFQKFIR GGIGTNNVDH CARLCHSSTV
AGLARAFGSG AMTNSIDEFK DARCIFVIGS NTPEAHPVIA IGIREAAVKN SAELIIADPR
EIELVRYAKL HMQQRPGSDV ALINAMMNVI LAEGLHDRDF IEERTEGFEE IVDAIKEMTP
EKAEKITTVP ADAIRQAART YARADSASIV FSMGITQHTT GTDNVLSLAN LAMLTGNVGK
ESAGVNPLRG QNNVQGACDL GALPNVYPGY QSVEDAEIHA KFEKAWDAKL SDKAGLTVVE
MFHAIEDGDV RALYLMGENP ALSDPNLNRT RKALEKVEFL VCQDVFLSES AQYADVVLPA
FSFAEKEGTF TNTERRIQRV RKAVDPPGQT RDDWIIVCDI ATAMGIPMQY ENTSQIMDEI
ASVSPIYGGI AYDRIEEVGL QWPCPDRDHP GTKYLHKGEF KRGKGKFHPV RFREPAELPS
KEFPLILSTG RQLYQYHTGT LSRKSPAIHQ KSPTGYVEIH FKDAKEYGIE DGDSVEVTTT
RGKVTTKASV GTQVAKGWLF MPFHFAEGPA NMLTNDALDP IAKIPELKVC AAKIRQL
//
