GenomeNet

Database: UniProt
Entry: M1YL70_NITG3
LinkDB: M1YL70_NITG3
Original site: M1YL70_NITG3 
ID   M1YL70_NITG3            Unreviewed;       519 AA.
AC   M1YL70;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00018198, ECO:0000256|HAMAP-Rule:MF_01025};
DE            EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973, ECO:0000256|HAMAP-Rule:MF_01025};
DE   AltName: Full=Alpha-IPM synthase {ECO:0000256|HAMAP-Rule:MF_01025};
DE   AltName: Full=Alpha-isopropylmalate synthase {ECO:0000256|HAMAP-Rule:MF_01025};
GN   Name=leuA {ECO:0000256|HAMAP-Rule:MF_01025,
GN   ECO:0000313|EMBL:CCQ91206.1};
GN   ORFNames=NITGR_590085 {ECO:0000313|EMBL:CCQ91206.1};
OS   Nitrospina gracilis (strain 3/211).
OC   Bacteria; Nitrospinae/Tectomicrobia group; Nitrospinota; Nitrospinia;
OC   Nitrospinales; Nitrospinaceae; Nitrospina.
OX   NCBI_TaxID=1266370 {ECO:0000313|EMBL:CCQ91206.1, ECO:0000313|Proteomes:UP000011704};
RN   [1] {ECO:0000313|EMBL:CCQ91206.1, ECO:0000313|Proteomes:UP000011704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3/211 {ECO:0000313|EMBL:CCQ91206.1,
RC   ECO:0000313|Proteomes:UP000011704};
RX   PubMed=23439773; DOI=10.3389/fmicb.2013.00027;
RA   Luecker S., Nowka B., Rattei T., Spieck E., and Daims H.;
RT   "The genome of Nitrospina gracilis illuminates the metabolism and evolution
RT   of the major marine nitrite oxidizer.";
RL   Front. Microbiol. 4:27-27(2013).
CC   -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC       with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-
CC       hydroxy-4-methylpentanoate (2-isopropylmalate). {ECO:0000256|HAMAP-
CC       Rule:MF_01025}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC         isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178,
CC         ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01025};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01025};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 1/4. {ECO:0000256|ARBA:ARBA00004689,
CC       ECO:0000256|HAMAP-Rule:MF_01025}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01025}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 1 subfamily. {ECO:0000256|ARBA:ARBA00009396,
CC       ECO:0000256|HAMAP-Rule:MF_01025}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCQ91206.1}.
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; CAQJ01000065; CCQ91206.1; -; Genomic_DNA.
DR   RefSeq; WP_005009593.1; NZ_HG422173.1.
DR   AlphaFoldDB; M1YL70; -.
DR   STRING; 1266370.NITGR_590085; -.
DR   HOGENOM; CLU_022158_0_1_0; -.
DR   InParanoid; M1YL70; -.
DR   OMA; NTMRMLV; -.
DR   OrthoDB; 9804858at2; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000011704; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
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   HAMAP; MF_01025; LeuA_type1; 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; IPR005671; LeuA_bact_synth.
DR   InterPro; IPR000891; PYR_CT.
DR   NCBIfam; TIGR00973; leuA_bact; 1.
DR   PANTHER; PTHR10277:SF9; 2-ISOPROPYLMALATE SYNTHASE 1, CHLOROPLASTIC-RELATED; 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:CCQ91206.1};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01025};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|HAMAP-Rule:MF_01025};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01025};
KW   Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430, ECO:0000256|HAMAP-
KW   Rule:MF_01025};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01025};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01025}; Reference proteome {ECO:0000313|Proteomes:UP000011704};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01025}.
FT   DOMAIN          6..268
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   REGION          394..519
FT                   /note="Regulatory domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT   BINDING         15
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT   BINDING         203
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT   BINDING         205
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT   BINDING         239
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
SQ   SEQUENCE   519 AA;  56457 MW;  485E7C1AB3DC8F79 CRC64;
     MQPERIIIFD TTLRDGEQCP GASMNNKEKL EIARQLSLLK VDVIEAGFPV ASPGDFESVK
     QIASEIRGSS VAGLARALNK DVEACARALE KAESPRIHIF LSTSKLHRDH KLNMDKGQII
     KMATDAIEFG RKYCDDIEFS PEDASRTEPD FLAEVVEAVI AAGAKTVNIP DTVGYSVPEQ
     FGALIHSLKE NVPNIDDAVI SVHCHNDLGM AVANSLAAVK AGARQVECTI NGIGERAGNA
     AMEEIVMALK TRKDFFGYDT RIDTSHIIAC SRLVSSLTGF FVQRNKAIVG KNAFAHESGV
     HQDGYLKKKD TYEIMDPRDI GLDSAELVLG KHSGRNALNK KIESMGYKLT VEEMDRVFSE
     FKVLADEKKD VYDEDILAVI QKQVTTDDSL NTYVLEKIQC GFETGVMPEA TVQLKSRDGQ
     THTATAQGDG PIDAIYNAMD KITGLTCKLL DYQVMSKTKG KDAQGEVSVR VLSENREVLG
     KGTGVNTVEA SGVAYVNAIN KLLLKSKSGP VDGNEIQGP
//
DBGET integrated database retrieval system