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Database: UniProt
Entry: I3YS58_AEQSU
LinkDB: I3YS58_AEQSU
Original site: I3YS58_AEQSU 
ID   I3YS58_AEQSU            Unreviewed;       287 AA.
AC   I3YS58;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Isopropylmalate/homocitrate/citramalate synthase {ECO:0000313|EMBL:AFL79826.1};
GN   OrderedLocusNames=Aeqsu_0312 {ECO:0000313|EMBL:AFL79826.1};
OS   Aequorivita sublithincola (strain DSM 14238 / LMG 21431 / ACAM 643 / 9-3).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Aequorivita.
OX   NCBI_TaxID=746697 {ECO:0000313|EMBL:AFL79826.1, ECO:0000313|Proteomes:UP000006049};
RN   [1] {ECO:0000313|EMBL:AFL79826.1, ECO:0000313|Proteomes:UP000006049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14238 / LMG 21431 / ACAM 643 / 9-3
RC   {ECO:0000313|Proteomes:UP000006049};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA   Munk A.C.C., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA   Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA   Faehnrich R., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Aequorivita sublithincola DSM 14238.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC       {ECO:0000256|ARBA:ARBA00009405}.
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DR   EMBL; CP003280; AFL79826.1; -; Genomic_DNA.
DR   RefSeq; WP_014781084.1; NC_018013.1.
DR   AlphaFoldDB; I3YS58; -.
DR   STRING; 746697.Aeqsu_0312; -.
DR   KEGG; asl:Aeqsu_0312; -.
DR   PATRIC; fig|746697.3.peg.311; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022138_3_2_10; -.
DR   OrthoDB; 9784013at2; -.
DR   Proteomes; UP000006049; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016833; F:oxo-acid-lyase activity; IEA:InterPro.
DR   CDD; cd07938; DRE_TIM_HMGL; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR043594; HMGL.
DR   InterPro; IPR000891; PYR_CT.
DR   PANTHER; PTHR42738; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR   PANTHER; PTHR42738:SF7; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          3..271
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   287 AA;  32058 MW;  FC928E585A09FD15 CRC64;
     MQQVKIIECP RDAMQGIKEW IPTEQKVQYL QSLLRCGFDT IDFGSFVSPK AIPQMQDTAE
     VLSKLDLSAT NSKLLAIIAN LRGAEDAVKH PEIDYLGYPF SISENFQMRN THKTIAESLV
     LLQEILNLAH KNNKEVVAYL SMGFGNPYGD PWNVEIVGEW TEKLSAMGVK ILSLSDTVGS
     STPDIISYLF SNLIPKYPHI EFGAHLHTTP NAWHEKVDAA YKAGCRRFDG AIQGFGGCPM
     AKDELTGNMP TEKMLSYFTA EKISCNINPM SFESAHNEAT KIFTKYH
//
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