ID   A0A1R4HBN8_9GAMM        Unreviewed;       512 AA.
AC   A0A1R4HBN8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Alpha-IPM synthase {ECO:0000256|ARBA:ARBA00029993};
GN   ORFNames=CRENPOLYSF1_450004 {ECO:0000313|EMBL:SJM93629.1};
OS   Crenothrix polyspora.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Crenotrichaceae; Crenothrix.
OX   NCBI_TaxID=360316 {ECO:0000313|EMBL:SJM93629.1, ECO:0000313|Proteomes:UP000195667};
RN   [1] {ECO:0000313|EMBL:SJM93629.1, ECO:0000313|Proteomes:UP000195667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSM_CP1 {ECO:0000313|EMBL:SJM93629.1};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000256|RuleBase:RU003523}.
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DR   EMBL; FUKI01000121; SJM93629.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R4HBN8; -.
DR   OrthoDB; 9803573at2; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000195667; Unassembled WGS sequence.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
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; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:SJM93629.1};
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:UP000195667};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          8..269
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   512 AA;  55811 MW;  E1C0D87AF4A92C4B CRC64;
     MSTQSRKIQL MDTTLRDGEQ TQGVSFTPTE KVSIAKALLQ SLRVDRIEVA SARVSEGEKE
     AVTSINTWAK QAGFAGCVEV LGFVDHTKSV DWILATGGNV INLLTKGSEK HCREQLGKTL
     AQHTDDIIRT VDYALQKNLT VNVYLEDWSN GYQNSPDYVY ELMNSLQHTG ISHFMLPDTL
     GVLSPEEVFV SLGDMCTRYP MLAFDFHPHN DYGLATANVM AAVRAGVSSI HCTINCLGER
     AGNASLAEVA VVLRDKMGLQ IAIDESHLAH VSNMVENFSG KRVAANAPII GADVFTQTAG
     IHADGDQKGG LYKTKLRPER FSRTHSYALG KMSGKASLKK NLEQLDLNLS EENQKKVLER
     IVSLGDSKQT ITTDDLPFII ADVLESKDYQ HIKLLNCSIT SGLNLESTAS IRVSIDGAKH
     TMTGSGNGGF SAFMDAISKV MQSHNYALPT LANYEVRIPK GGHTDALTEC VITWDCGGEL
     RKTRAVHANQ VFAGVLAALK IINMQLHELS QA
//