ID K0IKV7_NITGG Unreviewed; 511 AA.
AC K0IKV7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=2-isopropylmalate synthase {ECO:0000313|EMBL:AFU59172.1};
DE EC=2.3.1.182 {ECO:0000313|EMBL:AFU59172.1};
DE EC=2.3.3.13 {ECO:0000313|EMBL:AFU59172.1};
GN Name=leuA {ECO:0000313|EMBL:AFU59172.1};
GN OrderedLocusNames=Ngar_c22420 {ECO:0000313|EMBL:AFU59172.1};
OS Nitrososphaera gargensis (strain Ga9.2).
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrososphaerales;
OC Nitrososphaeraceae; Nitrososphaera.
OX NCBI_TaxID=1237085 {ECO:0000313|EMBL:AFU59172.1, ECO:0000313|Proteomes:UP000008037};
RN [1] {ECO:0000313|EMBL:AFU59172.1, ECO:0000313|Proteomes:UP000008037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ga9.2 {ECO:0000313|Proteomes:UP000008037};
RX PubMed=23057602; DOI=10.1111/j.1462-2920.2012.02893.x;
RA Spang A., Poehlein A., Offre P., Zumbragel S., Haider S., Rychlik N.,
RA Nowka B., Schmeisser C., Lebedeva E.V., Rattei T., Bohm C., Schmid M.,
RA Galushko A., Hatzenpichler R., Weinmaier T., Daniel R., Schleper C.,
RA Spieck E., Streit W., Wagner M.;
RT "The genome of the ammonia-oxidizing Candidatus Nitrososphaera gargensis:
RT insights into metabolic versatility and environmental adaptations.";
RL Environ. Microbiol. 14:3122-45(2012).
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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; CP002408; AFU59172.1; -; Genomic_DNA.
DR AlphaFoldDB; K0IKV7; -.
DR STRING; 1237085.Ngar_c22420; -.
DR KEGG; nga:Ngar_c22420; -.
DR PATRIC; fig|1237085.11.peg.2222; -.
DR HOGENOM; CLU_022158_0_1_2; -.
DR InParanoid; K0IKV7; -.
DR OrthoDB; 6555at2157; -.
DR Proteomes; UP000008037; Chromosome.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07940; DRE_TIM_IPMS; 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; IPR011830; LEU1_arch.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR02090; LEU1_arch; 1.
DR PANTHER; PTHR42880:SF2; (R)-CITRAMALATE SYNTHASE CIMA; 1.
DR PANTHER; PTHR42880; 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; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:AFU59172.1};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Reference proteome {ECO:0000313|Proteomes:UP000008037};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 15..266
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 511 AA; 55159 MW; B4A68A6F703A3C93 CRC64;
MSKANSNNNN DNNKVRIFDT TLRDGEQTPG VTVTPDQKVQ IAIKLDELGV DAIEAGFPIV
SQGEMQAVKT IANQGLKAEI CGLARATEAD INAAIKCDLK YVHTFIATSD IHMQYKLKMT
PEQVMDKAVK AVEYAKKHGM QVEFSAEDAT RSDRQFLLKV FKAVTDAGAD RIDIPDTVGY
RTPDYIAEIV RDVKSVTALP ISVHCHNDFG LAVANAIAGV NAGAACAHVT INGLGERAGN
ASLEEFVMAL EILYNKKHNI NTKLIYETSK FVSNAMGIIV QPNKAIIGEN AFGHESGIHT
HGIINNPLTY EPIAPELVGR KRWLQAGKHA GAHGIRAMLE DFGIKPTDEQ LKQIVEKQKN
IADKGKSITT SELLAIAGEI MGSTEFEEKF KLYDFHIVTG MNIIPTAVVR LNADGKDLIA
SNTGVGPVDA ALKAIQKIAG EVANVKIRDF MLDSITGGSD ALAVVTVKVE DKDGNIVSAK
KAGEDIVVAS VQAMMDAINK VLLRKVLYSK S
//
