ID F0RAZ7_CELLC Unreviewed; 504 AA.
AC F0RAZ7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=(R)-citramalate synthase {ECO:0000313|EMBL:ADY30574.1};
DE EC=2.3.1.182 {ECO:0000313|EMBL:ADY30574.1};
GN OrderedLocusNames=Celly_2757 {ECO:0000313|EMBL:ADY30574.1};
OS Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 /
OS NCIMB 1423 / VKM B-1433 / Cy l20).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY30574.1, ECO:0000313|Proteomes:UP000007487};
RN [1] {ECO:0000313|EMBL:ADY30574.1, ECO:0000313|Proteomes:UP000007487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 /
RC VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487};
RX PubMed=21677859; DOI=10.4056/sigs.1774329;
RA Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Mavromatis K., Ovchinikova G., Chen A.,
RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Brambilla E.M., Kannan K.P., Rohde M., Spring S., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Ivanova N.;
RT "Complete genome sequence of Cellulophaga lytica type strain (LIM- 21).";
RL Stand. Genomic Sci. 4:221-232(2011).
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|RuleBase:RU003523}.
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DR EMBL; CP002534; ADY30574.1; -; Genomic_DNA.
DR AlphaFoldDB; F0RAZ7; -.
DR STRING; 867900.Celly_2757; -.
DR KEGG; cly:Celly_2757; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_0_1_10; -.
DR Proteomes; UP000007487; Chromosome.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.30.160.340; -; 1.
DR Gene3D; 3.30.160.740; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR10277:SF57; (R)-CITRAMALATE SYNTHASE CIMA; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:ADY30574.1};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Reference proteome {ECO:0000313|Proteomes:UP000007487};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 5..265
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 504 AA; 56405 MW; 5ADD2E766AC622D6 CRC64;
MKRKIEIMDT TLRDGEQTSG VSFSVSEKLT LAKLLLEELK VDRIEVASAR VSDGELQAVQ
QITSWATAHN YINNVEVLTF VDKGVSIKWM QDAGAKVQNL LTKGSLNHLT HQLKKTPEQH
FKEIKETILL AQNHQIETNV YLEDWSNGMR NSKAYVYQFL DFLSHQPIKR VLLPDTLGVL
THTETFTYIS ELVKKYPNLH FDFHGHNDYD LSVANVMEAI KAGCHGLHLT INGMGERAGN
APMASVVAVI NDFLPDVEID LKETSLYKVS RLVSTFTGFG IPANKPIVGE NVFTQTAGIH
ADGDSKKNLY FNDLLPERFG RKRQYALGKT SGKANILKNL QELGLTLNDD DLGKVTQRII
ELGDKKEKVT KEDLPYIISD VLDSDSYQDK VIVKSYVLTH SKGLKPSTTV AVEIENELFE
ENAQGDGQYD AFMNAITKIF KAKNIKLPKL IDYAVRIPPG SNSDALCETI ITWQNGENEF
KTRGLDSDQT VSAIKATEKM LNII
//
