ID A0A0X7BBH0_9FLAO Unreviewed; 388 AA.
AC A0A0X7BBH0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN Name=leuA_1 {ECO:0000313|EMBL:KVV14760.1};
GN ORFNames=AP058_01813 {ECO:0000313|EMBL:KVV14760.1};
OS Flavobacterium sp. TAB 87.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1729581 {ECO:0000313|EMBL:KVV14760.1, ECO:0000313|Proteomes:UP000059935};
RN [1] {ECO:0000313|EMBL:KVV14760.1, ECO:0000313|Proteomes:UP000059935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAB87 {ECO:0000313|EMBL:KVV14760.1,
RC ECO:0000313|Proteomes:UP000059935};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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:KVV14760.1}.
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DR EMBL; LLWK01000036; KVV14760.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0X7BBH0; -.
DR STRING; 1729581.AP058_01813; -.
DR PATRIC; fig|1729581.3.peg.1875; -.
DR OrthoDB; 9804858at2; -.
DR Proteomes; UP000059935; Unassembled WGS sequence.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
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 Acyltransferase {ECO:0000313|EMBL:KVV14760.1};
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:UP000059935};
KW Transferase {ECO:0000256|RuleBase:RU003523, ECO:0000313|EMBL:KVV14760.1}.
FT DOMAIN 6..267
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 388 AA; 42517 MW; C2DA4E274B58F840 CRC64;
MNREKVQIFD TTLRDGEQVP GCKLDTKQKL VIAERLDQMG VDVIEAGFPV SSPGDFLSVS
EICKIVENAT VCGLTRAVKN DIDVAAAALK HAKRPRIHTG IGTSDSHIIH KLNTTREDII
ARAKFAVAHA KTYVEDVEFY AEDAGRTDNA FLAQVCEEVI KAGATVLNIP DTTGYCLPEE
YGAKIKYLKE NVKGIENVII SCHCHNDLGM ATANSIAGAV NGARQIECTI NGIGERAGNT
ALEEVVMIFK QHPYLNLDTN INTRQLNEMS RLVSESMGMM VQPNKAIVGA NAFAHSSGIH
QDGVIKNRAT YEIMDPLDVG VNESSIILTA RSGRAALAYR AKKVGYELTK VQLDLVYIEF
LKFADIKKEV IDEDIHQIVE ACRLEVCL
//
