ID A0A3M8PTS5_9GAMM Unreviewed; 960 AA.
AC A0A3M8PTS5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:RNF47308.1};
GN ORFNames=EBI00_15560 {ECO:0000313|EMBL:RNF47308.1};
OS Marinomonas hwangdonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=1053647 {ECO:0000313|EMBL:RNF47308.1, ECO:0000313|Proteomes:UP000280507};
RN [1] {ECO:0000313|EMBL:RNF47308.1, ECO:0000313|Proteomes:UP000280507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HDW-15 {ECO:0000313|EMBL:RNF47308.1,
RC ECO:0000313|Proteomes:UP000280507};
RX PubMed=22021582; DOI=10.1099/ijs.0.036582-0;
RA Jung Y.T., Oh T.K., Yoon J.H.;
RT "Marinomonas hwangdonensis sp. nov., isolated from seawater.";
RL Int. J. Syst. Evol. Microbiol. 62:2062-2067(2012).
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:RNF47308.1}.
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DR EMBL; RIZG01000016; RNF47308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8PTS5; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000280507; 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: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: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; 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.
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:UP000280507}.
FT DOMAIN 20..98
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 98..137
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 160..191
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 204..232
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 239..295
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 960 AA; 105046 MW; 756A2EA0D196FA61 CRC64;
MLQHFDPNKD YGTPAVQSDI QVTLEIDGIE ISVPEGTSVL RAAALANINI PKLCATDNLE
AFGSCRLCTV HIEGRRGAPA SCTTPAEQGM RVSTQNDKLA KLRRNIMELY ISDHPLDCLT
CPANGDCELQ DMAGAVGLRE VRYGFDGHNH LDAPKDTSNP YFTFDASKCI VCSRCVRACE
EVQGTFALTI DGRGFDSKVV AGQDESFFDS DCVSCGACVQ ACPTATLSEN AIITLGQPEH
SVVTTCAYCG VGCSFRAEMK GDQLVRMVPH KGGDANHGHS CVKGRFAFGY ATHKDRIKAP
MIRDSIDQPW REVSWEAAMA FAADRLTSIQ KEYGRESIGG ITSSRCTNEE TYLVQKLIRT
AFGNNNTDTC ARVCHSPTGY GLKQTLGESA GTQTFDSVMK SDCVLVIGAN PTDAHPVFGS
LMRRRLREGA SLIVADPRQI DLLKTPHLGA SLHLPLRPGT NVAMINALAH VVITEGLEDT
DFIAQRCDAS AYLRWRDFIK QSCHAPEVVE GITGVPAADI REAARTFAKV PNAAIYYGLG
VTEHSQGSTM VMGIANLALV TGNIGREGVG VNPLRGQNNV QGSCDMGSFP HELPGYQHVS
DPIARGRFEA VWGVTLDDEP GLRIPNMFDA AIAGQFRALY VQGEDIAQSD PNTQHVEEAL
RSLDCLIVQD IFLNETAKFA HVLLPGSTFL EKNGTFTNAE RRINRVRKVM PPVAGKEDWQ
VTMALSNALG YAMHYDHPSQ IMDEIAQLAP SFAGVSYDKL ELQGSLQWPC NDEFPDGSPI
MHETHFPTPH GKGQFAITEF VPTTERATRR FPLLLTTGRI LSQYNVGAQT RRTDNQRWHQ
EDVLELHPHD AEERGVKEGD WLGISSRAGR TVLRALISER MQPGVVYTTF HHPGSGANVI
TTNNSDWATN CPEYKVTAVQ VEKVSQPSEW QQGFEANHGR QQRFLLDATD SVAKDNYASK
//
