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Database: UniProt
Entry: A0A0B3SD98_9RHOB
LinkDB: A0A0B3SD98_9RHOB
Original site: A0A0B3SD98_9RHOB 
ID   A0A0B3SD98_9RHOB        Unreviewed;       965 AA.
AC   A0A0B3SD98;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:KHQ54696.1};
GN   ORFNames=OA50_00530 {ECO:0000313|EMBL:KHQ54696.1};
OS   Mameliella alba.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Mameliella.
OX   NCBI_TaxID=561184 {ECO:0000313|EMBL:KHQ54696.1, ECO:0000313|Proteomes:UP000030960};
RN   [1] {ECO:0000313|EMBL:KHQ54696.1, ECO:0000313|Proteomes:UP000030960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMTAT08 {ECO:0000313|EMBL:KHQ54696.1,
RC   ECO:0000313|Proteomes:UP000030960};
RA   Gan H.Y., Muhd D.-D., Mohd Noor M.E., Yeong Y.S., Usup G.;
RT   "Genome sequence of Ponticoccus sp. strain UMTAT08 isolated from clonal
RT   culture of toxic dinoflagellate Alexandrium tamiyavanichii.";
RL   Submitted (OCT-2014) 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:KHQ54696.1}.
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DR   EMBL; JSUQ01000002; KHQ54696.1; -; Genomic_DNA.
DR   RefSeq; WP_043137030.1; NZ_JSUQ01000002.1.
DR   AlphaFoldDB; A0A0B3SD98; -.
DR   STRING; 561184.SAMN05216376_107218; -.
DR   PATRIC; fig|1515334.3.peg.536; -.
DR   OrthoDB; 9816402at2; -.
DR   Proteomes; UP000030960; 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:UP000030960}.
FT   DOMAIN          21..99
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          99..138
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51839"
FT   DOMAIN          177..208
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          221..250
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          257..313
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   965 AA;  104947 MW;  8A69C660E012B3C2 CRC64;
     MKDFILPTDD RDMGTPARQG APVTLTIDGF EVTVPEGTSV MRAAAEIGIS VPKLCASDNL
     EAFGSCRLCA VEIEGRRGTP ASCTTPVAPG MVVDTQSQKV RKIRKGVMEL YISDHPLDCL
     TCAANGDCEL QDMAGAVGLR DVRYKAPDQG GLANHFEARN TSGEANPEWL PKDDSNPYFT
     YDPSKCIVCN RCVRACEEVQ GTFALTISGR GFDSRVSAGG VGDDFLASDC VSCGACVQAC
     PTATLQEKSV IEMGTPDRSV VTTCAYCGVG CSFKAEMQGD ELVRMVPYKH GKANRGHSCV
     KGRFAYGYAN HKDRILNPMI RDSIDEPWRE VSWDEALGFA AGRMRALQAK HGKKSIGVIT
     SSRCTNEETY LVQKLTRAVF GNNNTDTCAR VCHSPTGYGL GQTFGTSAGT QDFDSVEQTD
     VVIVIGANPT DGHPVFASRL KKRLRAGAKL IVIDPRRIDL VKSAHIEAAH HLALKPGTNV
     AVVTALAHVI VTEGLMDEAF IRTRCDWDEF QVYAEFVSDP RHSPEATALL TGVDAQELRA
     AARTFARGGN GAIYYGLGVT EHSQGSTTVM GIANLAMLTG NVGRPGVGVN PLRGQNNVQG
     SCDMGSFPHE LPGYRHVKLP EVREIFETTW GVEIDPEPGL RIPNMLDAAV EGTFKGLYCQ
     GEDILQSDPD TKHVAAGLAA MECVIVHDLF LNETANYAHV FLPGSTFLEK DGTFTNAERR
     INRVRRVMAP KNGYADWEVT QLLANAMGAG WSYTHPSQIM EEIAATTPSF AGVDYALLEE
     KGSVQWPCNE AHPEGTPLMH VDEFVRGKGR FIVTEYVATD EKTGPRFPLL LTTGRILSQY
     NVGAQTRRTE NVVWHEADVL EIHPHDAENR GLNDGDWVRL ASRSGETTLR AQVTDRVSPG
     VVYTTFHHPD TQANVITTDY SDWATNCPEY KVTAVQVAPS NGPTDWQEDY AAQAERSRRI
     LPAAE
//
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