ID A0A2T6BVK5_9FLAO Unreviewed; 390 AA.
AC A0A2T6BVK5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=C8N46_10798 {ECO:0000313|EMBL:PTX60092.1};
OS Kordia periserrulae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Kordia.
OX NCBI_TaxID=701523 {ECO:0000313|EMBL:PTX60092.1, ECO:0000313|Proteomes:UP000244090};
RN [1] {ECO:0000313|EMBL:PTX60092.1, ECO:0000313|Proteomes:UP000244090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25731 {ECO:0000313|EMBL:PTX60092.1,
RC ECO:0000313|Proteomes:UP000244090};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004689}.
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:PTX60092.1}.
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; QBKT01000007; PTX60092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6BVK5; -.
DR OrthoDB; 9804858at2; -.
DR Proteomes; UP000244090; Unassembled WGS sequence.
DR GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07940; DRE_TIM_IPMS; 1.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000891; PYR_CT.
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 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 Transferase {ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 6..267
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 390 AA; 42650 MW; CBAF0B10526F5FC8 CRC64;
MSSNRVYIFD TTLRDGEQVP GCKLNTEEKL MIAAKLDILG VDVIEAGFPV SSPGDFQSVE
AIAKLVKNAT VCGLTRAVQN DIKVAAEALK YAKRPRIHTG IGTSESHMKY KFKATPEQII
ERAVAAVKYA KSFVEDVEFY AEDAGRSDNK FLARVCEAVI KAGATVLNIP DTTGYCLPEE
YGQKIKYLKE NVAGIDNAIL SCHCHNDLGL ATANSIAGVM NGARQIECTI NGIGERAGNT
SLEEVTMILK QHPYLDLNTN INSKMLTEMS QLVSETMGMP VQPNKAIVGT NAFAHSSGIH
QDGVIKNRET YEIMDPKDVG AETSSIVLTA RSGRAALAYR AKNVGYNLTK RELDSVYSDF
LNFADKHKEV TDTDIHHIIK MSTTAKRMYA
//
