ID A0A193LJI4_9GAMM Unreviewed; 942 AA.
AC A0A193LJI4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=BA177_17220 {ECO:0000313|EMBL:ANO52700.1};
OS Woeseia oceani.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Woeseiaceae;
OC Woeseia.
OX NCBI_TaxID=1548547 {ECO:0000313|EMBL:ANO52700.1, ECO:0000313|Proteomes:UP000092695};
RN [1] {ECO:0000313|EMBL:ANO52700.1, ECO:0000313|Proteomes:UP000092695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XK5 {ECO:0000313|EMBL:ANO52700.1,
RC ECO:0000313|Proteomes:UP000092695};
RA Mu D., Du Z.;
RT "Complete genome sequence of a deep-branching marine Gamma Proteobacterium
RT Woeseia oceani type strain XK5.";
RL Submitted (JUN-2016) 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}.
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DR EMBL; CP016268; ANO52700.1; -; Genomic_DNA.
DR RefSeq; WP_068618280.1; NZ_CP016268.1.
DR AlphaFoldDB; A0A193LJI4; -.
DR STRING; 1548547.BA177_17220; -.
DR KEGG; woc:BA177_17220; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000092695; 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:UP000092695}.
FT DOMAIN 18..96
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 96..135
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 158..189
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 202..230
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 237..293
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 942 AA; 102785 MW; 7E9ED7097C4D928E CRC64;
MTVIREADLG TPASTATETV TVEIDGKALT VPVGTSVMRA ARGAGVDIPK LCATDSLKAF
GSCRLCVVEI EGRKGCPASC TTPVAEGMQI RTQSDGIAKL RRNVMELYIS DHPLDCLTCS
ANGDCELQDM AGAVGLRDVR YGMDGANHLD AKVDDSNPYF SFDPSKCIVC SRCVRACDEV
QGTFALTIEG RGFEAKVAAS SGESFLDSEC VSCGACVQAC PTATLMEKSI IEHGQPEHSV
LTTCAYCGVG CSFKADMQGD RVVRMTPYKD GQANHGHSCV KGRFAWGYAS HRERVLEPMI
RESIDEPWRK VSWDEAIGYA ATRLRGIQEK YGRKSVGGIT SSRCTNEEVF VVQKLVRAAF
GNNNVDTCAR VCHSPTGYGL NQTLGTSAGT QPFDSVMDAD VIVIIGANPT VAHPVFASQM
KRRLREGAKL IIIDPRRIDL VRSPHVQADY HLPLLPGTNV PVINALAHVI VSEGLVDQDY
VAQRCDPDSF AAWKACVLKE ENSPEAVAKI SGVAADDIRS AARLYATAGR GAIYYGLGVT
EHSQGSTMVM GMANLAMATG NIGFSGCGVN PLRGQNNVQG SCDMGSFPHE LAGYRPVSDD
AVRGSFEKRW GVELDPVPGY RIPNMFDAAI AGEYKGMYIQ GEDIAQSDPN TQHVEAALLA
MDCVVVQDLF LNETAKFAHV FLPGTSFLEK DGTFINAERR INRVRPVMKP QQGKAEWLIT
QELSQALGYD MHYASEAEIM DEIAALTPTF QGVSFDFLDR YGSVQWPCNE KAPLGTPIMH
IDQFVRGKGL FIETDYVPTE ERSNRKFPLL LTTGRILSQY NVGAQTRRTE NIVWYHEDLL
EIHPHDAETR GIQDGDQVSL RSRKGEITLR ATITERVQPG VVYTTFHNPE TGANVVTTEY
SDWATSCPEY KVTAVQVAPA ARRSEWQHKF AKRAAKQEVT ET
//
