ID A0A1I1ZJS7_9BACI Unreviewed; 541 AA.
AC A0A1I1ZJS7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN ORFNames=SAMN05192532_101285 {ECO:0000313|EMBL:SFE31957.1};
OS Alteribacillus iranensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacillus.
OX NCBI_TaxID=930128 {ECO:0000313|EMBL:SFE31957.1, ECO:0000313|Proteomes:UP000199516};
RN [1] {ECO:0000313|EMBL:SFE31957.1, ECO:0000313|Proteomes:UP000199516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23995 {ECO:0000313|EMBL:SFE31957.1,
RC ECO:0000313|Proteomes:UP000199516};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FONT01000001; SFE31957.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1ZJS7; -.
DR STRING; 930128.SAMN05192532_101285; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000199516; 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:UniProtKB-KW.
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 Reference proteome {ECO:0000313|Proteomes:UP000199516};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 5..267
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 541 AA; 59585 MW; 69D3D5531163E2EB CRC64;
MVSQVKLFDT TLRDGTQGEG ISLSVDDKLK IAAKLDQLGI HYIEGGWPGS NPKDMNFFER
VKDLKLKHSV VTAFGSTRRP GVTAEKDPNL NRIIESGAEA AAIFGKTWDF HVTEALQTTL
EENVSMIYDS VRFLKEKGLE VIFDAEHFFD GYKHNPEYAI KTIVAAENAG ADCVALCDTN
GGSLPTEIAD IITEVKKQVT IDVGIHCHND GELAVANTLE AVKAGAVHIQ GTTNGYGERC
GNANLISIIP NLQLKMGIPC VANEQLQQLT EVSKYIHELA NQTPPNGQPF TGKSAFAHKG
GMHVSAVLKH PETYEHIPPE KIGNERRVLV SELSGQSNLL FKAEELGISL DKGSPAIKET
IETIKEMEHK GYQYEAAEAS FELLIRNGLG ESHDYFEFEH FNIITHKERE NGFKSEAVVK
MKIQGQTVMT AAEGNGPVNA LDYALRKAIG EYYPLVHEMY LSDYKVRVLD EAEATASTVR
VLIESSDGQE TWSTIGVSPN VIEASWHALV DSIRYYFMKH SDRLTAVEPV AAMPEASVKN
H
//
