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Database: UniProt
Entry: M0AF25_9EURY
LinkDB: M0AF25_9EURY
Original site: M0AF25_9EURY 
ID   M0AF25_9EURY            Unreviewed;      1098 AA.
AC   M0AF25;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:ELY96472.1};
GN   ORFNames=C484_02130 {ECO:0000313|EMBL:ELY96472.1};
OS   Natrialba taiwanensis DSM 12281.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrialba.
OX   NCBI_TaxID=1230458 {ECO:0000313|EMBL:ELY96472.1, ECO:0000313|Proteomes:UP000011648};
RN   [1] {ECO:0000313|EMBL:ELY96472.1, ECO:0000313|Proteomes:UP000011648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12281 {ECO:0000313|EMBL:ELY96472.1,
RC   ECO:0000313|Proteomes:UP000011648};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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   -!- 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:ELY96472.1}.
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DR   EMBL; AOIL01000009; ELY96472.1; -; Genomic_DNA.
DR   RefSeq; WP_006824331.1; NZ_AOIL01000009.1.
DR   AlphaFoldDB; M0AF25; -.
DR   STRING; 1230458.C484_02130; -.
DR   PATRIC; fig|1230458.4.peg.417; -.
DR   OrthoDB; 23466at2157; -.
DR   Proteomes; UP000011648; Unassembled WGS sequence.
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:0015942; P:formate metabolic process; IEA:InterPro.
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; 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; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR   NCBIfam; TIGR01591; Fdh-alpha; 1.
DR   PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 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   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; 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.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE   4: Predicted;
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   NAD {ECO:0000256|ARBA:ARBA00023027}.
FT   DOMAIN          134..173
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51839"
FT   DOMAIN          196..229
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          240..269
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          389..447
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1074..1098
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1098 AA;  120205 MW;  6DD4D7CF2333C8B9 CRC64;
     MSSYNDPHPH VPNIDDPQPE TPLTEDFNKG TANDPNVDVT TTTTEITVDG ERLTMRPGST
     VLDAIEGTDA HQDVPALCHY ERGDEGDSGD HGRYEIGPRS ECRTCMVETD AYGLVPSCSF
     PAEDGLTVET DTADAMEARD VNLDLLLSNH NLRCTTCSKN GWCELQEASI QQGVEHPRYG
     VFDDRDEYEP IDSTSSFIQI DRNKCILCNR CVEACSDVQV AGVLRMEGNG PDTRIGFQSE
     AETMADSNCI SCGHCATVCP TGSIVEEGLT DMTTLPLPGF DQENSVGRVI HGERAETSET
     SSAPNRAVSG RSPTDVNVAR KSGVAKMMSR AKQQAGRTRK LASEKARETA EMVLEGTEHT
     AEFVAANSLP EGMLFDIGHA VGDQRLKRVT KAETTCGFCA VGCRFDLYGK DGEVLGTRPA
     DPDATPANGY STCVKGKFGY DFANSDERLE TPLIRRKDAP DGPAGPDGFR EASWDEALSR
     VVEELSETRE TYGQDSLAVF SSSKATNEEN FLMQKFARQV LGTKNIDNCT RLCHSSTVAA
     LKQTMGYGAM SNRIKDVGNA DCYLITGSNT TESHPVLATK LKQNVRDGAD LFVFEPRRIE
     LAEHADQFTR TAGGHDIAWI NGMIRHIIEN DLHDEAFIEE RTKGFEDVRE KVQSFTPEKV
     EELADVSPEE LANAAETIAE ADSCVFGWAM GISQHTYGTQ TVLALADLAL VTGNVGKPNA
     GVSPFRGQNN VQGGGGDMGT IPDNLPGYQD VSDDDVLDQF EEEWGVRPPD EPGLRVTEVF
     DEVDEGNVRG MYIIGENPAI SEPDVTNARE SLAELDFLVV QDIFMTETAE YADVILPAAT
     FTEKYGTVTN TERRVQLVRP AVDPPGSARA DWKILQELAR RMDFDWQYDS PTDIMDEVNE
     LTPIYGGITH ERLEEKGDGL QWPCPDEDHP GTPYLYEDEF NFEDGKARFI PADLGDPTEL
     PNEEFPIALT SGRVLYHWHT GQLTRRSEGL MGHVGESYAE IHPQTAGQIG VADGEYVEVE
     SKRGSIVVRA KVTERTAPGK IFIPMHFAQG AVNELTQEEL DPVSRIPDYK LASVRVSSMG
     PDPDTEPIGT PGPYSDDD
//
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