ID A0A099XRM7_9FLAO Unreviewed; 391 AA.
AC A0A099XRM7;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=PHEL85_3278 {ECO:0000313|EMBL:KGL59005.1};
OS Polaribacter sp. Hel1_85.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1250005 {ECO:0000313|EMBL:KGL59005.1, ECO:0000313|Proteomes:UP000029991};
RN [1] {ECO:0000313|EMBL:KGL59005.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel1_85 {ECO:0000313|EMBL:KGL59005.1};
RA Xing P., Hahnke R.L., Unfried F., Markert S., Huang S., Barbeyron T.,
RA Harder J., Becher D., Schweder T., Gloenk F.O., Amann R.I., Teeling H.;
RT "Niches of two polysaccharide-degrading Polaribacter strains isolated from
RT the North Sea during a spring diatom bloom.";
RL ISME J. 0:0-0(2014).
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:KGL59005.1}.
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DR EMBL; JPDS01000003; KGL59005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099XRM7; -.
DR STRING; 1250005.PHEL85_3278; -.
DR eggNOG; COG0119; Bacteria.
DR OrthoDB; 9804858at2; -.
DR Proteomes; UP000029991; 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:KGL59005.1};
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 Transferase {ECO:0000256|RuleBase:RU003523, ECO:0000313|EMBL:KGL59005.1}.
FT DOMAIN 6..267
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 391 AA; 42747 MW; 0E3FF55CED64959F CRC64;
MQDNKVQIFD TTLRDGEQVP GCKLDTTQKL VIAERLDLLG VNVIEAGFPV SSPGDFNSVT
QISKIVKNAT VCGLTRAVEN DIKVAAEALK YANYPRIHTG IGTSDSHIKF KFNSSREAVI
ERAIKAVSYA KSFVEDVEFY AEDAGRTDNE YLARVCEAVI KAGATVLNIP DTTGYCLPEE
YGAKMKYLRE NVKGIENVIL SCHCHNDLGM ATANSIAGVI NGARQIECTI NGIGERAGNT
ALEEVVMVLK QHPYLNLETS INTKLLYDTS IMVRESMGMP VQPNKAIVGA NAFAHSSGIH
QDGVIKNRET YEIMDPEDVG VTESAIVLTA RSGRAALAYR AKKIGYELTK VQLDIAYDAF
LETADKQKEV KDEDIHNIMK EVSKTSKVAT S
//
