ID J2TBP4_9PSED Unreviewed; 317 AA.
AC J2TBP4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Isopropylmalate/homocitrate/citramalate synthase {ECO:0000313|EMBL:EJM71819.1};
GN ORFNames=PMI29_01272 {ECO:0000313|EMBL:EJM71819.1};
OS Pseudomonas sp. GM49.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144331 {ECO:0000313|EMBL:EJM71819.1, ECO:0000313|Proteomes:UP000007288};
RN [1] {ECO:0000313|EMBL:EJM71819.1, ECO:0000313|Proteomes:UP000007288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM49 {ECO:0000313|EMBL:EJM71819.1,
RC ECO:0000313|Proteomes:UP000007288};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
CC -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC {ECO:0000256|ARBA:ARBA00009405}.
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:EJM71819.1}.
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DR EMBL; AKJL01000058; EJM71819.1; -; Genomic_DNA.
DR RefSeq; WP_007995067.1; NZ_AKJL01000058.1.
DR AlphaFoldDB; J2TBP4; -.
DR PATRIC; fig|1144331.3.peg.1223; -.
DR Proteomes; UP000007288; Unassembled WGS sequence.
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 4..279
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 317 AA; 34378 MW; 35DB52E6274BFFE1 CRC64;
MRDVILCECF ARDGLQHEPD FLPTHIKRRL VERFADIGFQ RIEATSYSNP AVIPQFADAS
ALLAVLQRRA GVFYKATCAN VRAVERAVMD LDAGLGANEI SLLVSASESH SRRNLKRSRA
DQWLNIEQMA DKALNQFRLI GTVSVAFGCP FEGRVSEASV LADVEQFAKH GVKFVTLGDT
TGVATPQSVR RLFGAVLASF PEITPIAHFH DTRATGLVNY VAALEVGVTH YDCAFGGVGG
HPAKVKYGGG HTGNVSTEDW INLLESMGVR TGIDLDRLLD VAAECEAALG RELHSRVLRS
GLNPLLHATV SPSDIIQ
//
