ID M0B5F8_NATA1 Unreviewed; 1094 AA.
AC M0B5F8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:ELZ06146.1};
GN ORFNames=C481_01400 {ECO:0000313|EMBL:ELZ06146.1};
OS Natrialba asiatica (strain ATCC 700177 / DSM 12278 / JCM 9576 / FERM
OS P-10747 / NBRC 102637 / 172P1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=29540 {ECO:0000313|EMBL:ELZ06146.1, ECO:0000313|Proteomes:UP000011554};
RN [1] {ECO:0000313|EMBL:ELZ06146.1, ECO:0000313|Proteomes:UP000011554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12278 {ECO:0000313|EMBL:ELZ06146.1,
RC ECO:0000313|Proteomes:UP000011554};
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:ELZ06146.1}.
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DR EMBL; AOIO01000003; ELZ06146.1; -; Genomic_DNA.
DR RefSeq; WP_006106984.1; NZ_AOIO01000003.1.
DR AlphaFoldDB; M0B5F8; -.
DR STRING; 29540.C481_01400; -.
DR PATRIC; fig|29540.5.peg.294; -.
DR eggNOG; arCOG01492; Archaea.
DR OrthoDB; 23466at2157; -.
DR Proteomes; UP000011554; 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; 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: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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011554}.
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..38
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 1065..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
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 1094 AA; 119929 MW; 875441EC8509A29E CRC64;
MSSYNDPHPH VPNIDDPQPE TPLTEDFNKG TANDPNVDVT TTATEITVDG ERLTMRPGST
VLDAIEGTDA HRDVPALCHY ERGDEGDSGD HGRYEIGPRS ECRTCMVETD AYGLVPSCSF
PAEDGLTVAT DTADAMEARD VNLDLLLSNH NLRCTTCSKN GWCELQDASI QQGVEHPRYG
VFDDRDEYEP IDSTSSFIQI DRNKCILCNR CVEACSDVQV AGVLRMEGNG PDTRIGFQSE
AETMSDSNCI SCGHCATVCP TGSIVEEGLT DMTTLPLPGF DQENSVGRVI HGERAETSET
SSAPNRAVSG RSPTDVNVAR KSGVAKMMSR AKQQAGRTRK LASEKARETA EMVLEGTEHT
AEFVAANSLP EGMLFDIGHA VGDQRLKRVN KAETTCGFCA VGCRFDLYGK DDEVLGTRPA
DPDATPANGY STCVKGKFGY DFANSDERLE TPLIKEDGEF REASWDEALS RVVEELSETR
ETYGQDSLAV FSSSKATNEE NFLMQKFARQ VLGTKNIDNC TRLCHSSTVA ALKQTMGYGA
MSNRIKDVGN ADCYLITGSN TTESHPVLAT KLKQNVRDGA DLFVFEPRRI ELAEHADQFT
RTAGGHDIAW INGMIRHIIE NDLHDEAFIE ERTKGFEDVE EKVQSFTPEK VEELTNVSPD
ELANAAETIA EADSCVFGWA MGVSQHTYGT QTVLALADLA LVTGHVGKPN AGVSPFRGQN
NVQGGGGDMG TIPDNLPGYQ DVTDDDVLDQ FEEEWGVRPP DEPGLRVTEV FDEVDEGNVR
GMYIIGENPA ISEPDVTNAR ESLQELDFLV VQDIFVTETA EYADVILPAA TFTEKYGTVT
NTERRVQLVR PAVEPPGSAR ADWKILQDLA RRMDFDWQYD SPTDIMDEVN ELTPIYGGIT
HDRLEENGDG LQWPCPDEDH PGTPYLYENE FNFEDGKARF VPADLGDPTE LPNEEFPIAL
TSGRVLYHWH TGQLTRRSEG LMGHVGESYA EIHPQTAGQI GVADDEYVKV ESKRGSIVVR
AKVTERTAPG KIFIPMHFAE GAVNELTQEK LDPVSRIPDY KMASVRVSSM GPDPDTEPIG
TPGETSPGTY SDDD
//
