ID A0A369WBL1_9GAMM Unreviewed; 954 AA.
AC A0A369WBL1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=DV711_10900 {ECO:0000313|EMBL:RDE19398.1};
OS Motiliproteus coralliicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Motiliproteus.
OX NCBI_TaxID=2283196 {ECO:0000313|EMBL:RDE19398.1, ECO:0000313|Proteomes:UP000253769};
RN [1] {ECO:0000313|EMBL:RDE19398.1, ECO:0000313|Proteomes:UP000253769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C34 {ECO:0000313|EMBL:RDE19398.1,
RC ECO:0000313|Proteomes:UP000253769};
RA Wang G.;
RT "Motiliproteus coralliicola sp. nov., a bacterium isolated from Coral.";
RL Submitted (JUL-2018) 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=[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: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005404}.
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:RDE19398.1}.
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DR EMBL; QQOH01000003; RDE19398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369WBL1; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000253769; 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; cd00508; MopB_CT_Fdh-Nap-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; 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:UP000253769}.
FT DOMAIN 22..100
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 100..139
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 162..193
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 204..233
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 240..296
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 954 AA; 104862 MW; 4B6BB31ADB284583 CRC64;
MLEHFDPAQE KDLGTPAVIS DTLVELAIDG IPVQVPEGTS VLRAAALAGI TIPKLCASDN
LDAFGSCRLC AVQVEGRRGY PASCTTPAED GMQVTTQNSK LAKLRRNIME LYISDHPLDC
LTCPSNGDCE LQDMAGAVGL REVRYGFDGH NHLDAEKDLS NPYFSFDPAK CIVCSRCVRA
CEEVQGTFAL NVNGRGFDSK ITAGNRDFMA SDCVSCGACV QSCPTSTLME NSVIEQGQPE
RSVVTTCAYC GVGCSFKAEL KGDQLVRMVP YKGGEANHGH GCVKGRFAFG YATHKDRIRT
PMIRDSLDEP WREVSWEQAI EHTAARFKAI QAEHGRNSVS GITSSRCTNE ETYLVQKLIR
AAFGNNNTDT CARVCHSPTG YGLKQTLGES AGTQTFDSAM DADVIMVIGA NPTDAHPVFG
SVLRRRLRQG AKLIVADPRK IDLLKTASLG ESQHLPLLPG TNVALINALA HVVISEGLED
QDFIAKRCDD EQYQQWREFI LDEQNSPERM AAVTGLSAEA IRQAARTYAN ADNSAIFYGL
GVTEHSQGST MVMGIANLAM ATGNIGRSGV GVNPLRGQNN VQGSCDMGSF PHELPGYQPV
GDDQIRARFE QSWGVSLDPE PGMRIPNMFN AALEGSLKGM YVQGEDLAQS DPNTQHVEAA
LKALDFLVVQ DIFLNETAKF AHVLLPGASF LEKDGTFTNA ERRINRVRKV MPPLAGKADW
EVTMDLSNAL GYPMNYQHPS EIMDEIATLV PTFKGVSYDK LERLGSIQWP CNDENPDGMP
IMHVEDFPIG KGRFVLTEFV PTTERCSRRF PLLLTTGRVL SQYNVGAQTR RTANQAWHDE
DRLDIHPQDA EDRGINDGDW LGISSRAGDT VLRARISERM QPGVVYTTFH HPESGANVIT
TDNSDWATNC PEYKVTAVQV EKVSQPSRWQ QEFRQLRERQ SELLKRRKRE PQQG
//
