ID A0A0S8C215_9PROT Unreviewed; 606 AA.
AC A0A0S8C215;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=2-oxoglutarate oxidoreductase {ECO:0000313|EMBL:KPK17521.1};
GN ORFNames=AMJ67_13270 {ECO:0000313|EMBL:KPK17521.1};
OS Betaproteobacteria bacterium SG8_41.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1703391 {ECO:0000313|EMBL:KPK17521.1, ECO:0000313|Proteomes:UP000051544};
RN [1] {ECO:0000313|EMBL:KPK17521.1, ECO:0000313|Proteomes:UP000051544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_41 {ECO:0000313|EMBL:KPK17521.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK17521.1}.
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DR EMBL; LJTT01000053; KPK17521.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8C215; -.
DR STRING; 1703391.AMJ67_13270; -.
DR PATRIC; fig|1703391.3.peg.1683; -.
DR Proteomes; UP000051544; 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; IPR033412; PFOR_II.
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; PF17147; PFOR_II; 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}.
FT DOMAIN 6..191
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 224..418
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 485..556
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 606 AA; 66042 MW; 048EF48E8B382312 CRC64;
MVSDSGEGAQ RCGQSLGSIA ARMGNGVWTV EIIPAEIQPP ARSIEGASGN RIRLGAKRVS
NGGNETDLVV AFNEQVLIGR VRAGELKPGC TILLESAWRE HSDPKIAASY TETHDRLVTD
GYKVIEIPME QECRKHVSDP RRGKNMFALG MLCSIYSLDL QLAREQIVFA FGKKNESVVK
SNITLLEAGY EWAEANLEFK YRIPAAPVKE PQIVVNGNTA LALGVLASGM EVCAMYPITP
ATSASHYLSE AFESVGGIVH QAEDEIAACA FAIGASYAGK CAVTITSGPG YSLKQEAIGL
AVMCEIPLVV VNVQRGGPST GQPTKAEQGD LLTACFGSHG DAPKVVMAPA TIEDCFYSII
TARKIAETFN VVVVVLSDAN LATSQQPFSR PQFADTWLAP PVDQSAVDEG TKPYDWDPVT
GLARRLVPGQ PHGMHTLTGL AHDRASRVAY NPEINEEAIR HRSLKIAALQ KTLKAPPVFG
GDSGDLLLIG WGSTKGAIEE TVERLREEGH KVSSMHLTFL QPMPAGIKEI MQRFRRVMTI
ESNWCDRLED AIIDETNRRY SALALMLRAR YLVDIDCWSE VKGQPIKPGT IYRVIREKLE
KERRKT
//
