ID Q7N5R1_PHOLL Unreviewed; 665 AA.
AC Q7N5R1;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Photorhabdus luminescens subsp. laumondii TTO1 complete genome segment 7/17 {ECO:0000313|EMBL:CAE14176.1};
GN OrderedLocusNames=plu1883 {ECO:0000313|EMBL:CAE14176.1};
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01) (Photorhabdus luminescens subsp. laumondii).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265 {ECO:0000313|EMBL:CAE14176.1, ECO:0000313|Proteomes:UP000002514};
RN [1] {ECO:0000313|Proteomes:UP000002514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01
RC {ECO:0000313|Proteomes:UP000002514};
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
CC -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC CO(2). {ECO:0000256|ARBA:ARBA00003906}.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; BX571865; CAE14176.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7N5R1; -.
DR STRING; 243265.plu1883; -.
DR KEGG; plu:plu1883; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_012907_2_1_6; -.
DR Proteomes; UP000002514; Chromosome.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002514};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 343..519
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 665 AA; 73636 MW; 5278C4AE1BA3ABF5 CRC64;
MIDVQINEVP LKEHSPSIND CLDEQKLLYD MLLSREFDNR SAIVTRQGRA WFHVSAAGHE
GLAVLPQLME KNDVLVPYYR DRALVLARGM SIVEMTRELM GKATSHSAGR TMSNHFCSKE
HNIFSVVSLT GTQCIPAAGA AWASVLDNKN GLVVCGVGDA ATRQGEFYEA VSFAVEKRLP
VVFVVSDNKL GISTSTEKMA PYRLGIFNEC LIRRVDARKP ETLFTVAQEV FNKARFERTP
CILVCRMDRL DSHSNSDSHK LYRTPDELEV LQDPIENYVA YLKEKGAITE QALAEQKERI
KADVAEIFER VYHEEEPDPA SVSTYLCNRE GTPTVHVEME AEETQVKAVN QVLDEALSQH
PNVLIFGEDI EDPKGGVFGF TRGLSTRYPD RVINAPLSEA TIIGSSVGLS ASGWRPIVEL
QFIDFVGLGL NQLQSQLGTL SWRTVGKWRC PVVIYAPYGA YLPGGGIWHS QSSDGILAHI
PGINVLVPTT PADTVALFRT ALSLDMPSLI LIPKHLMRER HERRLVSPVS LGQANIVRAG
KDITLVAWGN TTQLATMAAL QAEKDNIDIE VIELRSLVPW DKQRIAESLR KTGRLIVVQE
DTRTASVGAS IIADILDEND NFFSLLAPPR LVTREDIHIP FNPCLEKAVL PGTDDILASV
YAVMS
//
