ID A0A0F7JJ69_9DEIO Unreviewed; 395 AA.
AC A0A0F7JJ69;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=homocitrate synthase {ECO:0000256|ARBA:ARBA00012974};
DE EC=2.3.3.14 {ECO:0000256|ARBA:ARBA00012974};
GN ORFNames=SY84_02355 {ECO:0000313|EMBL:AKH16076.1};
OS Deinococcus soli (ex Cha et al. 2016).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=1309411 {ECO:0000313|EMBL:AKH16076.1, ECO:0000313|Proteomes:UP000034024};
RN [1] {ECO:0000313|EMBL:AKH16076.1, ECO:0000313|Proteomes:UP000034024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N5 {ECO:0000313|EMBL:AKH16076.1,
RC ECO:0000313|Proteomes:UP000034024};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Deinococcus soli/N5/whole genome sequencing.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA +
CC H(+); Xref=Rhea:RHEA:12929, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58884; EC=2.3.3.14;
CC Evidence={ECO:0000256|ARBA:ARBA00000523};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12930;
CC Evidence={ECO:0000256|ARBA:ARBA00000523};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 1/5.
CC {ECO:0000256|ARBA:ARBA00004755}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. Homocitrate synthase LYS20/LYS21 subfamily.
CC {ECO:0000256|ARBA:ARBA00006361}.
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DR EMBL; CP011389; AKH16076.1; -; Genomic_DNA.
DR RefSeq; WP_046842651.1; NZ_JAVDTP010000001.1.
DR AlphaFoldDB; A0A0F7JJ69; -.
DR KEGG; dch:SY84_02355; -.
DR PATRIC; fig|1309411.5.peg.494; -.
DR OrthoDB; 9804858at2; -.
DR UniPathway; UPA00033; UER00028.
DR Proteomes; UP000034024; Chromosome.
DR GO; GO:0004410; F:homocitrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR CDD; cd07948; DRE_TIM_HCS; 1.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR048253; DRE_TIM_HCS_fun_bact.
DR InterPro; IPR011872; Homocitrate_synth.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR02146; LysS_fung_arch; 1.
DR PANTHER; PTHR10277:SF48; HOMOCITRATE SYNTHASE, CYTOSOLIC ISOZYME-RELATED; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Reference proteome {ECO:0000313|Proteomes:UP000034024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 21..278
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 395 AA; 43566 MW; 69A56DE0DEA0B459 CRC64;
MTQDPSVTTD HPAPLIPATS WAIIDSTLRE GEQFARGNFK QGDKIEIARA LDAFGAEFIE
VTTPMVSAQT HADIRRLTGL GLKAKFLTHV RCHMDDVQRA VDTGVDGLDL LFGTSSFLRE
FSHGKNIGQI IDSAQQVISW IKTNHPDLQI RFSAEDTFRS EEADLMAVYK AVSDLGVHRV
GLADTVGVAT PRQVYTLVRE VRKVIHAECG IEFHGHNDTG CAVSNAYEAV EAGATHIDTT
ILGIGERNGI TPLGGFLARM FTFDPQGLID KYNLDLLPEL DRMIARMVDL PIPWNNYLTG
EFAYNHKAGM HLKAIYLNPG AYEAIPPGVF GVGRRIQAAS KVTGKHAIAY KAREMGLHYG
EDALRRVTDH IKALAEQDEL DDAHLEQVLR EWVSA
//