ODHI_CORGL
ID ODHI_CORGL Reviewed; 143 AA.
AC Q8NQJ3; Q6M5D9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Oxoglutarate dehydrogenase inhibitor;
GN Name=odhI; OrderedLocusNames=Cgl1441, cg1630;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2] {ECO:0000312|EMBL:CAF21450.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025 {ECO:0000312|EMBL:CAF21450.1};
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-19, IDENTIFICATION, FUNCTION, PHOSPHORYLATION AT
RP THR-14, AND MUTAGENESIS OF THR-14.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025 {ECO:0000269|PubMed:16522631};
RX PubMed=16522631; DOI=10.1074/jbc.m512515200;
RA Niebisch A., Kabus A., Schultz C., Weil B., Bott M.;
RT "Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase
RT activity via the phosphorylation status of the OdhI protein.";
RL J. Biol. Chem. 281:12300-12307(2006).
CC -!- FUNCTION: An essential component of the PknG signaling pathway. When
CC unphosphorylated, it inhibits the activity of 2-oxoglutarate
CC dehydrogenase. When phosphorylated it does not inhibit 2-oxoglutarate
CC dehydrogenase. {ECO:0000269|PubMed:16522631}.
CC -!- INTERACTION:
CC Q8NQJ3; Q8NRC3: odhA; NbExp=2; IntAct=EBI-7868645, EBI-7868591;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR EMBL; BA000036; BAB98834.1; -; Genomic_DNA.
DR EMBL; BX927152; CAF21450.1; -; Genomic_DNA.
DR RefSeq; NP_600658.1; NC_003450.3.
DR RefSeq; WP_003856253.1; NC_006958.1.
DR PDB; 2KB3; NMR; -; A=1-143.
DR PDB; 2KB4; NMR; -; A=1-143.
DR PDB; 4QCJ; X-ray; 2.00 A; A=1-143.
DR PDBsum; 2KB3; -.
DR PDBsum; 2KB4; -.
DR PDBsum; 4QCJ; -.
DR AlphaFoldDB; Q8NQJ3; -.
DR BMRB; Q8NQJ3; -.
DR SMR; Q8NQJ3; -.
DR DIP; DIP-48322N; -.
DR IntAct; Q8NQJ3; 3.
DR MINT; Q8NQJ3; -.
DR STRING; 196627.cg1630; -.
DR iPTMnet; Q8NQJ3; -.
DR World-2DPAGE; 0001:Q8NQJ3; -.
DR GeneID; 58309366; -.
DR KEGG; cgb:cg1630; -.
DR KEGG; cgl:Cgl1441; -.
DR PATRIC; fig|196627.13.peg.1408; -.
DR eggNOG; COG1716; Bacteria.
DR HOGENOM; CLU_108862_1_0_11; -.
DR OMA; IGKFRLT; -.
DR EvolutionaryTrace; Q8NQJ3; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR CDD; cd00060; FHA; 1.
DR DisProt; DP01581; -.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16522631"
FT CHAIN 2..143
FT /note="Oxoglutarate dehydrogenase inhibitor"
FT /id="PRO_0000272962"
FT DOMAIN 68..117
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:16522631"
FT MUTAGEN 14
FT /note="T->A: Inhibition of growth on glutamine and
FT glutamate degradation."
FT /evidence="ECO:0000269|PubMed:16522631"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:2KB3"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:2KB4"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:2KB3"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2KB3"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:4QCJ"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:4QCJ"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:4QCJ"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:4QCJ"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:4QCJ"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:2KB4"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:4QCJ"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:4QCJ"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:4QCJ"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:4QCJ"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:4QCJ"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:4QCJ"
SQ SEQUENCE 143 AA; 15402 MW; 1AFFC8459842FCDD CRC64;
MSDNNGTPEP QVETTSVFRA DLLKEMESST GTAPASTGAE NLPAGSALLV VKRGPNAGAR
FLLDQPTTTA GRHPESDIFL DDVTVSRRHA EFRINEGEFE VVDVGSLNGT YVNREPRNAQ
VMQTGDEIQI GKFRLVFLAG PAE
