ID A0A1U7D510_9RHOB Unreviewed; 973 AA.
AC A0A1U7D510;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Formate dehydrogenase alpha subunit {ECO:0000313|EMBL:APX23229.1};
DE EC=1.2.1.2 {ECO:0000313|EMBL:APX23229.1};
GN ORFNames=Ga0080559_TMP2433 {ECO:0000313|EMBL:APX23229.1};
OS Salipiger profundus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1229727 {ECO:0000313|EMBL:APX23229.1, ECO:0000313|Proteomes:UP000186559};
RN [1] {ECO:0000313|EMBL:APX23229.1, ECO:0000313|Proteomes:UP000186559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT2016 {ECO:0000313|EMBL:APX23229.1,
RC ECO:0000313|Proteomes:UP000186559};
RA Tang K.;
RT "Deep-sea bacteria in the southern Pacific.";
RL Submitted (MAR-2016) 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}.
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DR EMBL; CP014796; APX23229.1; -; Genomic_DNA.
DR RefSeq; WP_076623352.1; NZ_FOLR01000011.1.
DR AlphaFoldDB; A0A1U7D510; -.
DR STRING; 1229727.Ga0080559_TMP2433; -.
DR KEGG; tpro:Ga0080559_TMP2433; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000186559; 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: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 Oxidoreductase {ECO:0000313|EMBL:APX23229.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186559}.
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 185..216
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 229..258
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 265..321
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 973 AA; 106146 MW; 56ABB46209AEFD03 CRC64;
MKDFIIPWDD RDKGTPAASG KPVHLTIDGI RVTVPAGTSV MRAAAEAGIT VPKLCATDSL
DAFGSCRLCV VEIEGRRGTP ASCTTPVHEG MKVHTQSSKV KKIRKGVMEL YVSDHPLDCL
TCAANGDCEL QDMAGMVGLR DVRYTPGENH YDPSGTGARS QAEARLRMPE GEANPRYMPK
DESNPYFTYD PSKCIVCSRC VRACEEVQGT FALTIQGRGF ESRVSAGASG DDFLASDCVS
CGACVQACPT ATLQEKSVAE LGTPDREVVT TCAYCGVGCS FKAELNGDQL VRMTPWKHGK
ANRGHSCVKG RFAYGYAEHP DRILNPMIRD SIDEPWREVS WDEALDFAAG RLKRIQETHG
RRSVGVITSS RCTNEETYLV QKLTRAVFRN NNTDTCARVC HSPTGYGLGQ TFGTSAGTQD
FDSVEKVDVA VVIGANPTDG HPVFASRLKK RLRQGAKLIV IDPRRIDLVK SAHIEAAHHL
PLTPGTNVAV VTALAHVIVT EGLYDEAFIR ERCDWDEFQA FAEFVSDRRH APESTALLTG
VNAAELRAAA RLFATGGNGA IYYGLGVTEH SQGSTTVMAL ANLAMMTGNI GREGVGVNPL
RGQNNVQGSC DMGSFPHELP GYRHVKLPEV RKVFEDAWGV EIDPEPGLRI PNMLDAAVEG
SFKGLYCQGE DILQSDPDTH HVAAGLRAMD CVIVHDLFLN ETANYAHVFL PGSSFLEKNG
TFTNAERRIN RVRKVMAPKN GYEDWEVTQL LANAMGAGWS YTDPAQIMAE IAATTPSFAG
VSYGLLEEKG SVQWPCNEDH PEGTPMMHVD GFVRGKGRFI VTEYVATDEK TGPRFPLLLT
TGRILSQYNV GAQTRRTANS VWHEADLLEV HPHDAENRGL RDGDWVRLAS RSGETTLRVK
ITDRVSPGVV YTTFHHPDTQ ANVVTTDFSD WATNCPEYKV TAVQVSPSNG PTDWQEDYAA
QAARSRRILP AAE
//
