ID A0A1S2VEE5_9BACT Unreviewed; 506 AA.
AC A0A1S2VEE5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=2-isopropylmalate synthase {ECO:0000313|EMBL:OIN56566.1};
GN ORFNames=BLX24_24160 {ECO:0000313|EMBL:OIN56566.1};
OS Arsenicibacter rosenii.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Arsenicibacter.
OX NCBI_TaxID=1750698 {ECO:0000313|EMBL:OIN56566.1, ECO:0000313|Proteomes:UP000181790};
RN [1] {ECO:0000313|EMBL:OIN56566.1, ECO:0000313|Proteomes:UP000181790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM-1 {ECO:0000313|EMBL:OIN56566.1,
RC ECO:0000313|Proteomes:UP000181790};
RA Huang K.;
RT "Arsenicibacter rosenii gen. nov., sp. nov., an efficient arsenic-
RT methylating bacterium isolated from an arsenic-contaminated paddy soil.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|RuleBase:RU003523}.
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:OIN56566.1}.
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DR EMBL; MORL01000021; OIN56566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S2VEE5; -.
DR OrthoDB; 9804858at2; -.
DR Proteomes; UP000181790; Unassembled WGS sequence.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.238.260; -; 1.
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; 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:UP000181790};
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 506 AA; 56609 MW; 3717694CB3FB1E24 CRC64;
MSRLIEIMDT TLRDGEQTSG VSFSASEKLT IAQLLLKEVK VDRLEVASAR VSDGEFQAVK
KITRWAQENG CIDKIEVLTF VDGDTSVNWM IDAGAKVMNL LTKGSMNHLI HQLKKTPEQH
FREIEQVISL ARSKDIRCNV YLEDWSNGMR NSPDYVFQFL DFLTRQPVDR VLLPDTLGVL
TPHETYTFIK SIVDRYPNSH FDFHAHNDYD LSIANVMEAV RAGANGLHLT VNGMGERAGN
APLASAIAAL NDFMPEVKTS VVETSLYSVS KLVETFTGFR IPANKPVVGE NVFTQTAGIH
ADGDNKNNLY FNDLMPERFG RTRKYALGKT SGKANIEKNL QELGIKLSAA DLKKVTQRII
ELGDRKEMVT REDLPYIISD ILDSNSIEEK VVVVNYVLTH SKGLRPSATL QVQIKGQLYE
ENAQGDGQYD AFMNALKKIY QRLKMPLPML TDYTVRIPPG GKTDALCETI ITWSINDKEV
KTRGLDSDQT VSAIKATQKM LNLLAI
//
