ID G4QMZ8_GLANF Unreviewed; 968 AA.
AC G4QMZ8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN OrderedLocusNames=GNIT_3323 {ECO:0000313|EMBL:AEP31417.1};
OS Glaciecola nitratireducens (strain JCM 12485 / KCTC 12276 / FR1064).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Glaciecola.
OX NCBI_TaxID=1085623 {ECO:0000313|EMBL:AEP31417.1, ECO:0000313|Proteomes:UP000009282};
RN [1] {ECO:0000313|EMBL:AEP31417.1, ECO:0000313|Proteomes:UP000009282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 12485 / KCTC 12276 / FR1064
RC {ECO:0000313|Proteomes:UP000009282};
RX PubMed=22123761; DOI=10.1128/JB.06296-11;
RA Bian F., Qin Q.L., Xie B.B., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA Chen X.L., Zhou B.C., Zhang Y.Z.;
RT "Complete genome sequence of seawater bacterium Glaciecola nitratireducens
RT FR1064T.";
RL J. Bacteriol. 193:7006-7007(2011).
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}.
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DR EMBL; CP003060; AEP31417.1; -; Genomic_DNA.
DR RefSeq; WP_014110288.1; NC_016041.1.
DR AlphaFoldDB; G4QMZ8; -.
DR STRING; 1085623.GNIT_3323; -.
DR KEGG; gni:GNIT_3323; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_0_6; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000009282; Chromosome.
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:UP000009282};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075}.
FT DOMAIN 33..111
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 111..150
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 173..204
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 217..246
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 253..309
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 968 AA; 106224 MW; 747A673FAE5B485E CRC64;
MVNYFNPATD IVAPQPKFDV NKDYGTPPSE STETVNIQVD GVTITVAEGT SVLRAAALAD
INIPKLCASD NLTAFGSCRL CAVQIEGMRG YPASCTTPVK EGMVVTTQND DIGKLRRNIM
ELYISDHPLD CLTCSSNGDC ELQDMAGAVG LREVRYGFDG DNHLDAKIDD SNPYFTFEPS
KCITCSRCVR ACEEVQGTFA LTIEGRGFKS KVSAGTSEEN FISSDCVSCG ACVQACPTAT
LMEKSVIDKG QPEHSVITTC AYCGVGCSFK AEMKGEEVIR MVPYKGGKAN QGHSCVKGRF
AFGYATHKDR ITEPMIRDSI DQPWREVSWE EAIAFSADKI KGIQAKYGRD SVGGITSSRC
TNEETYLVQK LIRAAFGNNN TDTCARVCHS PTGYGLKATI GESAGTQTFE SVMKSDVIMV
IGANPTDAHP VFASLLRKRL RQGAELIVVD PRSIDLLNTA HISANHHLAL RPGTNVAMIN
AIAHVVISEG LEDKQFIENR TDEYNAWREF ILDDINSPEA MAEITTVDAE EIRKAARIFA
KAKNGAIYYG LGVTEHSQGS TMVMGIANLA LATGNIGREG VGINPLRGQN NVQGSCDMGS
FPQELPGYQH VSDNALRAKF EKSWGVTLDN EPGFRIPNMF DAAIEGTFKA MYVQGEDILQ
SDPNTQHVQA ALSSLECLIV QDIFLNETAM YAHVFLPGSS FLEKDGTFTN AERRINRVRK
VMKPLAKYAD WEVTQMLSNA LGYPMNYQHP SEIMDEIASL VPTFSRVNYK KLDEQGSIQW
PCNDEFPDGS PIMHVEHFPI GNGRFAITPY LGSEDRANRR FPLLLTTGRI LSQYNVGAQT
RRTANQSWHQ EDLLEIHPND ADERGIKDGD WLGITSRAGD TVLRAKVSDR MKNGVVFTTF
HHPISGANVI TTDSSDWATN CPEYKVTAVQ VEKVSSPSAW QTRYKDFTKK QKGPFNQSTE
AESKTIGS
//
