ID A0A0W0V961_9GAMM Unreviewed; 605 AA.
AC A0A0W0V961;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:KTD16397.1};
GN Name=korA {ECO:0000313|EMBL:KTD16397.1};
GN ORFNames=Ljor_0703 {ECO:0000313|EMBL:KTD16397.1};
OS Legionella jordanis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=456 {ECO:0000313|EMBL:KTD16397.1, ECO:0000313|Proteomes:UP000055035};
RN [1] {ECO:0000313|EMBL:KTD16397.1, ECO:0000313|Proteomes:UP000055035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL-540 {ECO:0000313|EMBL:KTD16397.1,
RC ECO:0000313|Proteomes:UP000055035};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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:KTD16397.1}.
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DR EMBL; LNYJ01000011; KTD16397.1; -; Genomic_DNA.
DR RefSeq; WP_058470254.1; NZ_RDQQ01000015.1.
DR AlphaFoldDB; A0A0W0V961; -.
DR STRING; 456.Ljor_0703; -.
DR PATRIC; fig|456.5.peg.744; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000055035; 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:UP000055035}.
FT DOMAIN 16..203
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 254..439
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 500..568
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 605 AA; 65719 MW; 5ECDB227FCE6156D CRC64;
MPNTDSIVIR LTGDSGDGVQ LVGEQLTIAA ALTGRDVRTL PDFPAEIRAP AGTVAGISGF
QLAMSEQAIF TAGESLDVLV ALNPAALKNS LQHLNPGGLL IINEDSFQAK DWQKANLDQE
ILNNAAEYYQ ILSLPLITQT LQAVNGLDIN HAQAKKAKNF YVLGLVLWLF DLPVENCLQF
IRKKFKANVE IAKANELTLL AGYNYAMTLE LSRREFMLGQ VGRHQGEYRQ ITGVEAIGLA
IASLATLTET SVLVSGYPIT PASAILQECV RLKDFGVHLL QAEDEIAAIC ACIGASFGGQ
LALTCTSGPG FDLKAESLGL AVMAELPLVL LDVQRAGAST GLPTKTGQSD LHQALYGRHG
EAPLPVLAAQ SPADCFNTVV EAFRIAVKYM TPVIVLLDAY LANAAEPWKL PEVESIEVPK
LKFNRFPKPY QRDEFLSRSW NIPGTAGFIQ QIGGLEKQGE EGRVSYDAEN HQKMVMLRAN
KITGIAREYR PVEIEGDENA KILLIGWGST YGSLRSAINQ CREEGIEIAL IHLRHLNPLP
SDLADLIAKF ETVLVAELNS GHLCQLLRAT YLVNAKSITQ CNGQPFAVSH LVKAIKLEIN
HEPNL
//