ID A0A166U1R3_9EURY Unreviewed; 774 AA.
AC A0A166U1R3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:KZN26311.1};
GN ORFNames=A4G99_21105 {ECO:0000313|EMBL:KZN26311.1};
OS Haladaptatus sp. R4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haladaptataceae; Haladaptatus.
OX NCBI_TaxID=1679489 {ECO:0000313|EMBL:KZN26311.1, ECO:0000313|Proteomes:UP000076599};
RN [1] {ECO:0000313|EMBL:KZN26311.1, ECO:0000313|Proteomes:UP000076599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R4 {ECO:0000313|EMBL:KZN26311.1,
RC ECO:0000313|Proteomes:UP000076599};
RA Mukhopadhyay S.K.;
RT "Genome sequence of halophilic archaea.";
RL Submitted (APR-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=[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:KZN26311.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LWHG01000002; KZN26311.1; -; Genomic_DNA.
DR RefSeq; WP_066138195.1; NZ_LWHG01000002.1.
DR AlphaFoldDB; A0A166U1R3; -.
DR STRING; 1679489.A4G99_21105; -.
DR OrthoDB; 246365at2157; -.
DR Proteomes; UP000076599; Unassembled WGS sequence.
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; 3.40.50.740; -; 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; 2.
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}.
FT DOMAIN 70..127
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 753..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 774 AA; 85155 MW; C8BF350290DFF38D CRC64;
MTDDDTEKKG VAGFMARAKE QAQTASRKLD GSEAFQPVEH VAESFAANTM SEGRLFDMAD
ALSVYRLSDV DVTDTTCGYC AVGCRFDVYS KDDEVLGIRP NPEKAPINGI STCVKGKFGY
KYANSDDRLT EPLIKEDGEF REASWDEALD RVAEGLSEIQ DEYGRNGVSF VSSSKTSNEA
NYLMQKLARQ VFGTNNIDNC NRLCHSPTVA GLSQTVGFGA GSVGVEALEN ADCYLITGSN
TTEAHPVIAT RIKQNVKDGA DMFVFDPRKV QIAQFATQYS RVQPGYDTVW INGLTRHIIE
NDLHDEEFIE ERTVGFDELK EGLEKFTPEF VEEKTGVPPE ELERAAETVA NADSCVFCWT
LGLTEHSHGT ENVISMANLA LVTGHVGTEH SGLAPFRGQN NVQGGGGDMG PLPGNFPGYQ
KVTTDDAREK FEDAYGVELP DEEGYTITEQ FLAADRGEIR GMFIEGENVV YSEPNVAHAE
EIVENLEFLA VQDIFLTDTA KYADVVLPAN SPFETNGTYT SSTRHVQLVK RAIDPPGNAK
PDWVITQELA ERFGYDWGFR NPSEIMDEVN DLTPIYGGIT HERLETEGSI PWPCWDEDHP
GTPYLYDEEF NTADGKAHMI PTHVSGPVEA DMDDEDFPLA MTTGRVLYQY HTGTMTNRDA
GIRSYTDELF VEINPATAEE LGVSDAQYVD VTSRKGSITA LAQVTERPGE GVVFVPMHYF
GQGGAANELT DEEHLDDQAH VPEFKVTDVR ITPAETKPDV DVSERAATDG GRTD
//
