ID H8GQT3_METAL Unreviewed; 504 AA.
AC H8GQT3;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Alpha-IPM synthase {ECO:0000256|ARBA:ARBA00029993};
GN ORFNames=Metal_3415 {ECO:0000313|EMBL:EIC31068.1};
OS Methylomicrobium album BG8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomicrobium.
OX NCBI_TaxID=686340 {ECO:0000313|EMBL:EIC31068.1, ECO:0000313|Proteomes:UP000005090};
RN [1] {ECO:0000313|EMBL:EIC31068.1, ECO:0000313|Proteomes:UP000005090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BG8 {ECO:0000313|EMBL:EIC31068.1,
RC ECO:0000313|Proteomes:UP000005090};
RX PubMed=23580712;
RA Kits K.D., Kalyuzhnaya M.G., Klotz M.G., Jetten M.S., Op den Camp H.J.,
RA Vuilleumier S., Bringel F., Dispirito A.A., Murrell J.C., Bruce D.,
RA Cheng J.F., Copeland A., Goodwin L., Hauser L., Lajus A., Land M.L.,
RA Lapidus A., Lucas S., Medigue C., Pitluck S., Woyke T., Zeytun A.,
RA Stein L.Y.;
RT "Genome Sequence of the Obligate Gammaproteobacterial Methanotroph
RT Methylomicrobium album Strain BG8.";
RL Genome Announc. 1:E0017013-E0017013(2013).
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|RuleBase:RU003523}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001475; EIC31068.1; -; Genomic_DNA.
DR AlphaFoldDB; H8GQT3; -.
DR STRING; 686340.Metal_3415; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_0_1_6; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000005090; Chromosome.
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 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:UP000005090};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 1..259
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 504 AA; 55324 MW; DBEE66DF026964C4 CRC64;
MDTTLRDGEQ TQGVSFTPAE KVNIAKALLQ WLRVDRIEVA SARVSQGEKE AVASINAWAR
QEGFAGRVEV LGFVDHTRSV NWILETGGSV INLLTKGSEK HCREQLGKTL EQHTQDIRQT
IDYALQKGLK VNVYLEDWSN GYQNSPDYVF GLMDNLKDAG ISHFMLPDTL GVMAPDEVFA
SIGDMCRRYP ALRFDFHPHN DYGLATANVM AAVRAGVSSV HCTVNCLGER AGNASLAEVA
VVLRDKMAME LSIDETHIVR ISQMVENFSG KRIAANAPVI GSDVFTQTAG IHADGDHKGG
LYKTRLSPER FSRTRSYALG KMSGKASLKK NLELLEVDLS EENQKKVLAR IVQLGDSKQT
ITTEDLPFII ADVLESKSYE HIRLLNCSIT SGLHLESTAS LRVEVNGGKH QTSGSGNGGF
DAFIDALDKV LKLHDYTLPA LADYEVRIPK GGHTDALTEC VITWDCGSEL RKTRGVHANQ
VFAGVMATLK IINMQLHELK ASQV
//
