ID A0A2V1P4M2_9RHOB Unreviewed; 966 AA.
AC A0A2V1P4M2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:PWG17365.1};
GN ORFNames=DFK10_06180 {ECO:0000313|EMBL:PWG17365.1};
OS Salibaculum griseiflavum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salibaculum.
OX NCBI_TaxID=1914409 {ECO:0000313|EMBL:PWG17365.1, ECO:0000313|Proteomes:UP000245293};
RN [1] {ECO:0000313|Proteomes:UP000245293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WDS4C29 {ECO:0000313|Proteomes:UP000245293};
RA Du Z., Wang X.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:PWG17365.1}.
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DR EMBL; QETF01000005; PWG17365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1P4M2; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000245293; 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; 2.
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:UP000245293}.
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 178..209
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 222..251
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 258..314
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 966 AA; 105470 MW; CB2F9499E0F47084 CRC64;
MKDFIIPTDD RDMGTPASKS DKMVTLTIDG FDVQVPEGTS VMRASAEAGI QVPKLCATDS
LEAFGSCRLC VVEIEGRRGT PASCTTPVAD GMVVHTQSSK VRRIRKGVME LYISDHPLDC
LTCAANGDCE LQDMAGAVGL RDVRYEEPKA GGFVNHFEAR DTGGDVNPQY LPKDDSNPYF
TYDPSKCIVC SRCVRACEEV QGTFALTIEG RGFDSRVSAG AAGDDFLTSD CVSCGACVQA
CPTATLQEKS VIEMGTPERS VITTCAYCGV GCSFKAELQG DDLVRMVPYK HGKANRGHSC
VKGRFAYGYA NHADRILNPM IRDSIDEPWR EVSWEEAIGF AAQKMRGLQD KYGKKSIGVI
TSSRCTNEET FLVQKLARAV FGNNNTDTCA RVCHSPTGYG LGQTYGTSAG TQDFDSVEET
DVAIVIGANP TDGHPVFASR LKKRLRQGAK LIVIDPRRID LVKSNHIKAA HHLALRPGTN
VAVVTALAHV IVTEGLYDEA YIRERCDWDE FQHYVEFVSD ARHSPEATEM LTGVPAEDLR
AAARTYATGG RGSIYYGLGV TEHSQGSTTV MGIANLAMLT SNVGGNGMGV NPLRGQNNVQ
GSCDMGSFPH ELPGYRHVKN PEVRDLFKQA WGVEIDPEPG LRIPNMLDAA VDGTFKGLYC
QGEDILQSDP DTKHVAAGLA AMECVIVHDL FLNETANYAH VFLPGSSFLE KDGTFTNAER
RINRVREVMK PRNGYADWEV TQLLANAMGA GWTYTHPSQI MDEISATTPS FAGVSYEVLE
EKGSVQWPCN EAHPDGTPLM HVDGFVRGKG RFMITEYVAT DEKTGPRFPL LLTTGRILSQ
YNVGAQTRRT DNVVWHHEDV LEIHPHDAEV RGVNEGDFVK LASRSGETTL RATLTDRVSP
GVVYTTFHHP DTQANVITTD YSDWATNCPE YKVTAVQVSP SNGPTEWQED YNAQAAQSRR
ILPAAE
//
