ID A0A0Q9Z164_9COXI Unreviewed; 622 AA.
AC A0A0Q9Z164;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=2-oxoglutarate oxidoreductase subunit KorA {ECO:0000313|EMBL:KRG22801.1};
DE EC=1.2.-.- {ECO:0000313|EMBL:KRG22801.1};
GN Name=korA {ECO:0000313|EMBL:KRG22801.1};
GN ORFNames=HT99x_00342 {ECO:0000313|EMBL:KRG22801.1};
OS Candidatus Berkiella aquae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Berkiella.
OX NCBI_TaxID=295108 {ECO:0000313|EMBL:KRG22801.1, ECO:0000313|Proteomes:UP000051497};
RN [1] {ECO:0000313|EMBL:KRG22801.1, ECO:0000313|Proteomes:UP000051497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HT99 {ECO:0000313|EMBL:KRG22801.1,
RC ECO:0000313|Proteomes:UP000051497};
RA Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.;
RT "Draft Genome Sequences of Two Novel Amoeba-resistant Intranuclear
RT Bacteria, Candidatus Berkiella cookevillensis and Candidatus Berkiella
RT aquae.";
RL Submitted (SEP-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:KRG22801.1}.
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; LKAJ01000001; KRG22801.1; -; Genomic_DNA.
DR RefSeq; WP_075064979.1; NZ_LKAJ02000001.1.
DR AlphaFoldDB; A0A0Q9Z164; -.
DR STRING; 295108.HT99x_00342; -.
DR PATRIC; fig|1590043.3.peg.343; -.
DR Proteomes; UP000051497; 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 ECO:0000313|EMBL:KRG22801.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051497}.
FT DOMAIN 32..219
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 269..479
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 521..591
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 622 AA; 67878 MW; E3300FC39638036E CRC64;
MTDMKTFTTT IPLTVKRIPL EKVVIHFAGD SGDGMQVAGM QFTEACATFG NDVRTFPDFP
AEIRAPAGTL PGVSGFQLSF SEHPIHTPGD QYDVLVAMNP AALKVSLKNL KKGGILILDE
DKFTSKDLKK AQIDDNSLDG TLSAFRVVRL PMTTLTLTAL EKSPLSRAAA RKCKNMFALG
VVFWLYHREL EDTKDWIKER FKDKTDVIEA NIEALRAGYH FAITTELFAE HFSVKAAKQA
PGIYRQITGN QALAWGCVAA ATKANQSLLV CGYPITPASD ILHFLAKHAH FGVKTFQAED
EIAAIGAAIG AAFGGELTLT TTSGPGMDLK SEALGLAVMT ELPLVVVDVQ RAGPSTGMPT
KVEQSDLLAA MYGRHGECPV PILAPATPGD CFHIMLEAFR IALRYMTPVI VLSDAFLANG
AEPWQIPDVK TLPDLKPHYC QPTDNFMPYA RDPNTLARPW AIPGTKGLEH RIGGLEKENG
SGNISYDGDN HQRMVDIRAA KVQGIAQDLP LLELMGPKQG EVLILSWGST YGAVRTVVES
LQTQGHAISF AHLRYLNPFQ NELGSLLQQF KTILVVELNK GQLCQLIRAR YLVDAKGINK
VQGKPFGVQE LTEKVLPYLE KN
//
