ID A0A497XQN0_9AQUI Unreviewed; 539 AA.
AC A0A497XQN0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:RLJ70449.1};
GN ORFNames=BCF55_0724 {ECO:0000313|EMBL:RLJ70449.1};
OS Hydrogenivirga caldilitoris.
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Hydrogenivirga.
OX NCBI_TaxID=246264 {ECO:0000313|EMBL:RLJ70449.1, ECO:0000313|Proteomes:UP000267841};
RN [1] {ECO:0000313|EMBL:RLJ70449.1, ECO:0000313|Proteomes:UP000267841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16510 {ECO:0000313|EMBL:RLJ70449.1,
RC ECO:0000313|Proteomes:UP000267841};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:RLJ70449.1}.
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; RCCJ01000001; RLJ70449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A497XQN0; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000267841; Unassembled WGS sequence.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR022367; 2-oxoacid/accept_OxRdtase_asu.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR NCBIfam; TIGR03710; OAFO_sf; 1.
DR PANTHER; PTHR32154:SF20; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORA; 1.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000267841}.
FT DOMAIN 11..135
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 184..411
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
SQ SEQUENCE 539 AA; 59273 MW; A47633380201A908 CRC64;
MDKTIIIGGK AGAGIKEAGR MLLGVLANLG YHAFGYVDYP SLIRGGHNFV SLRFSEKPVY
SVDKKADVII ATDGRSIQAH LQDAKEDTVW VINEKEKLEG AIQVPFKEVA PGFFKSSSVL
GAVLKLFGIP LEEGLPFILS LPEREKNEQI YRDAYQATPT VFELKKAGER KGDVLTGNEC
IALGAVDGGL EFYIAYPMTP ASPVLHYLAE RKGEFGIKVI HPENEIGVIN MAVGVAFAGK
RAMVGTSGGG FALMTETLSL IGMSETPMVI YEAQRAGPST GVPTYTGQSD LLFCMFAGHG
DFPRVVLAPA TPEEAYRLTR DALNIAWKFQ VPVLILGDKH LGESYYLSKV RREKLVEEPK
LWEGNGEYKR YAVTEDGISP LAFPGAEGII VKGTSYEHDE RGITVEDALS VKKMQDKRLR
KGETLREYIL SREDTVAVGG VKGSDRVLIT WGSTEGTALD VAEEMGFKVV RSVFLEPFPE
ERLKQEIEGA NLVISLECSA SGQFEKLLKM HGITPHRSLK KYDGRPFFRD ELIDILREV
//
