ID A0A2C9CM56_9RHOB Unreviewed; 541 AA.
AC A0A2C9CM56;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN ORFNames=SAMN06273572_101139 {ECO:0000313|EMBL:SOH92297.1};
OS Monaibacterium marinum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Monaibacterium.
OX NCBI_TaxID=1690039 {ECO:0000313|EMBL:SOH92297.1, ECO:0000313|Proteomes:UP000220034};
RN [1] {ECO:0000313|EMBL:SOH92297.1, ECO:0000313|Proteomes:UP000220034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 {ECO:0000313|EMBL:SOH92297.1,
RC ECO:0000313|Proteomes:UP000220034};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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; OCTN01000001; SOH92297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9CM56; -.
DR OrthoDB; 9803573at2; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000220034; Unassembled WGS sequence.
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 6..273
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 541 AA; 58267 MW; A68270B414B20CF2 CRC64;
MTREPLSLFD TTLRDGQQTH GVDFSLDDKR RIAQALDDLG LGYVEGGWPG ANPTDSDFFD
AAPKLKNATF TAFGMTKRAG RSAANDDVLA GVLNAGTPAV CLVGKSHDFH VTTALGITLD
ENRENIRESF AHIVAQGRET LFDAEHFFDG YKANPDYALA CLHEAYNAGC RWIVLCDTNG
GTLPDEIGRI VGAVIASGIP GANLGIHTHN DTENAVAGSL AAVDAGARQI QGTLNGLGER
CGNANLISLI PTLLLKEPYA SKYDIGIPRE KLASLTTVSR MLDDILNRVP NRHAAYVGAS
AFTHKAGLHA SAILKDPTTY EHVVPEEVGN ARVVPMSNQA GQSNLRKRLE EAGIAVEKGD
PRLGQILDEI KRREDQGYAY DSAKGSFELI ARGILGQLPQ FFDVERYRVI VEKRRNAKGD
KITVSEAVVV VNIAGERIIS AADSFYADSE ADQGPVHALS AALQRDLGQY QSLIDDMKLV
DFKVRITNGG TEAVTRVLID SEDGQGRRWS TVGVSANIVD ASFQALSDAV TWKLIRDGAK
A
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