ID H8G9U6_9PSEU Unreviewed; 536 AA.
AC H8G9U6;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN ORFNames=SacazDRAFT_03737 {ECO:0000313|EMBL:EHY90599.1};
OS Saccharomonospora azurea NA-128.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=882081 {ECO:0000313|EMBL:EHY90599.1};
RN [1] {ECO:0000313|EMBL:EHY90599.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA-128 {ECO:0000313|EMBL:EHY90599.1};
RX PubMed=22768365; DOI=10.4056/sigs.2635833;
RA Klenk H.P., Held B., Lucas S., Lapidus A., Copeland A., Hammon N.,
RA Pitluck S., Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G.,
RA Land M., Ivanova N., Rohde M., Goker M., Detter J.C., Kyrpides N.C.,
RA Woyke T.;
RT "Genome sequence of the soil bacterium Saccharomonospora azurea type strain
RT (NA-128(T)).";
RL Stand. Genomic Sci. 6:220-229(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+);
CC Xref=Rhea:RHEA:19045, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30934, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.21;
CC Evidence={ECO:0000256|ARBA:ARBA00034270};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from pyruvate: step 1/3. {ECO:0000256|ARBA:ARBA00004743}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|ARBA:ARBA00006154, ECO:0000256|RuleBase:RU003523}.
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DR EMBL; CM001466; EHY90599.1; -; Genomic_DNA.
DR RefSeq; WP_005444090.1; NZ_CM001466.1.
DR AlphaFoldDB; H8G9U6; -.
DR HOGENOM; CLU_022158_7_0_11; -.
DR OrthoDB; 9803573at2; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000004705; Chromosome.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR CDD; cd07941; DRE_TIM_LeuA3; 1.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.30.160.270; -; 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; IPR005675; Citramal_synthase.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR00977; citramal_synth; 1.
DR PANTHER; PTHR43538:SF1; (R)-CITRAMALATE SYNTHASE; 1.
DR PANTHER; PTHR43538; ALPHA-IPM SYNTHASE/HOMOCITRATE SYNTHASE; 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 15..282
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 536 AA; 56999 MW; 985A3220FF9420FF CRC64;
MNRTEPAGTP LGDQFHLYDT TLRDGAQREG ISYSITDKLA VARLLDDLGV GFIEGGWPGA
LPKDTEFFAR AAAGELTLRH AVLVAFGSTR RAGIAVADDP QVRALLESQA PVVTLVAKSD
ARHIERALRV DVDEACAMVR DTVSFLVREG RRVFVDAEHF FDGYAHDPDT ALRVLDAAGQ
AGADVVVLCD TNGGQLPLGI AETVREVAER TGLRLGIHCQ DDTACAVANS IAAVQAGATH
VQCTANGYGE RAGNADLFAV TGNLVAKLGM PVLPEGRVAE LTRTAHALAE LANLAPEEHQ
AYVGTSAFAH KAGLHASAIK VDPLLYNHID PELVGNDMRV LVTEMAGRAS LELKGRQLGV
DLADKPEALS GALKKVKALE AEGWSFEAAD ASLELLLRAE ADDAPVEAPF RLESYRVVLE
HRSGGDVVSE ATVRVHVGGE RVIATAEGNG PVHALDAALR QSLRGHLSWL DSVELSDYKV
RILVGKPGTD AVTRVLVEST DGDRTWTTVG VHPNIVEASW LALCDALVHK SLTVSH
//
