ID A0A078L3H6_9GAMM Unreviewed; 605 AA.
AC A0A078L3H6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=2-oxoglutarate oxidoreductase subunit KorA {ECO:0000313|EMBL:CDZ78679.1};
GN Name=korA {ECO:0000313|EMBL:CDZ78679.1};
GN ORFNames=BN59_02991 {ECO:0000313|EMBL:CDZ78679.1};
OS Legionella massiliensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1034943 {ECO:0000313|EMBL:CDZ78679.1, ECO:0000313|Proteomes:UP000044071};
RN [1] {ECO:0000313|EMBL:CDZ78679.1, ECO:0000313|Proteomes:UP000044071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Urmite Genomes Urmite Genomes;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CCSB01000003; CDZ78679.1; -; Genomic_DNA.
DR RefSeq; WP_044011796.1; NZ_CCVW01000003.1.
DR AlphaFoldDB; A0A078L3H6; -.
DR STRING; 1034943.BN59_02991; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000044071; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000044071}.
FT DOMAIN 16..203
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 253..450
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 500..590
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 605 AA; 65260 MW; 423FFE2A8C0C1A5C CRC64;
MPNRDSIVIR LTGDSGDGVQ LVGEQLTITA ALTGRDVRTL PDFPAEIRAP AGTVAGVSGF
QLAMAEQAIF TAGEELDVLV ALNPAALKHS LEHLNPGGLL IINEDSFSEK DWQKAGLNPD
VLDKAAEHYH LVALPLVTQT LKAVESLDIS HAQAKKAKNF YVLGLVLWLF DLPTDSCLAF
ITKKFKANQQ IAKANELTLL AGYNYAMTLE LSRRQFMLGQ VSRDNGEYRQ ITGVEAVALA
LATLAVSTKI PLFVSGYPIT PASAILHESA KLADYGVQLL QAEDEIAAIC SCIGAAYGGC
LALTCTSGPG LDLKSESLGL AVMTELPLVL LDIQRAGAST GLPTKTGQSD LRQALYGRHG
EAPLPVLAAK SSADCFNTII EAFTLATKYM TPVIVLLDAY LANAAEPWKI PAVESIKIPE
INFNRFPKPY QRDELLTRSW NVPGTAGFIH QIGGLEKQGE EGRVSYDAEN HQKMVKLRAD
KVAGISRDYA ELTIEGDENA KTLVIGWGST YGSLKSAVNQ CHAEGLALAL VHLRHLNPLP
ADLARLLTKF DRILVAELNS GQLCQLLRAT YLVDAKSINQ CNGQPFTVSH LVTAIKLEAN
YEQQL
//
