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
//