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Database: UniProt
Entry: A0A0U5H3T3_9EURY
LinkDB: A0A0U5H3T3_9EURY
Original site: A0A0U5H3T3_9EURY 
ID   A0A0U5H3T3_9EURY        Unreviewed;       703 AA.
AC   A0A0U5H3T3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Formate dehydrogenase alpha subunit {ECO:0000313|EMBL:CQH58238.1};
DE            EC=1.2.1.2 {ECO:0000313|EMBL:CQH58238.1};
GN   Name=fdhA {ECO:0000313|EMBL:CQH58238.1};
GN   ORFNames=HHUB_2705 {ECO:0000313|EMBL:CQH58238.1};
OS   Halobacterium hubeiense.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=1407499 {ECO:0000313|EMBL:CQH58238.1, ECO:0000313|Proteomes:UP000066737};
RN   [1] {ECO:0000313|Proteomes:UP000066737}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JI20-1 {ECO:0000313|Proteomes:UP000066737};
RX   PubMed=26628271; DOI=10.1111/1462-2920.13130;
RA   Jaakkola S.T., Pfeiffer F., Ravantti J.J., Guo Q., Liu Y., Chen X., Ma H.,
RA   Yang C., Oksanen H.M., Bamford D.H.;
RT   "The complete genome of a viable archaeum isolated from 123-million-year-
RT   old rock salt.";
RL   Environ. Microbiol. 18:565-579(2016).
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR   EMBL; LN831302; CQH58238.1; -; Genomic_DNA.
DR   RefSeq; WP_059057129.1; NZ_LN831302.1.
DR   AlphaFoldDB; A0A0U5H3T3; -.
DR   STRING; 1407499.HHUB_2705; -.
DR   GeneID; 26659336; -.
DR   KEGG; hhb:Hhub_2705; -.
DR   OrthoDB; 23466at2157; -.
DR   Proteomes; UP000066737; Chromosome I.
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:0015942; P:formate metabolic process; IEA:InterPro.
DR   CDD; cd02753; MopB_Formate-Dh-H; 1.
DR   Gene3D; 2.40.40.20; -; 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; 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; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   NCBIfam; TIGR01591; Fdh-alpha; 1.
DR   PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   PIRSF; PIRSF000144; CbbBc; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PE   4: Predicted;
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:CQH58238.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000066737}.
FT   DOMAIN          4..61
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   703 AA;  76989 MW;  C3147A650888C41A CRC64;
     MSTDESTKTI CPYCGVGCGI SVRQGDEPGD VSFAPWGEAP VNEGRVCIKG GAATEVVDHE
     DRLTEPMIRE DGDLRPASWD EALSRVVAEM EDIRDEHGPD GMGFYASSKT MNEENYLLQK
     LARRFGTNNV DNCTRMCHAS TVYALRESLG AGAMTNSMAD LRDEADVFWI QGANPGEQHP
     IANSQYFRQA VLDGATVIQV DPHANKTTES FEIEESDRHM HLQLEPGTDI PLLNAVLKTV
     LDNGWVDEEF VAERTEGIED LRETLADFDK EAAAEECGVP LEDIERAAEA YATADNAAIF
     TGMGMSQHAC GVDNVQNEIN LALATGNLGR PGTGVNPLRG QNNVQGASDV GAMPNVLPGY
     QPVDDDEARE AVEDVWGFEI PSEPGLTNVE ITHSVGDTVH GLYVMGENPV MSEPNADRVA
     DLLDETEFVV VQDIFPTETV EYADVVLPAT TWAERGGTVT NTDRRVQRMR GVEKVHEDTR
     HDLDILTEVG TRLFGEDAGF DFDGPEEVFE ELREVCPIYH GMTYDALGEE GLHWPCYEPG
     DEGDQFLYAD SFDTPSGRGQ IEGVRHQPPR ETPDDEYPLI LTTARLEEHY NTGTMSRRSA
     TLSRQHPENF VDVHPEDAER FGVADGDSVT LRSRRGEITL RANVTEAIKE GVVWTTPHFA
     DASANVLTND VLDERAKIPE YKAAAVDVTL ADGGADPDAP ADD
//
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