ID A0A0U5H4U4_9EURY Unreviewed; 399 AA.
AC A0A0U5H4U4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-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};
DE AltName: Full=Alpha-IPM synthase {ECO:0000256|ARBA:ARBA00029993};
GN Name=leuA1 {ECO:0000313|EMBL:CQH59774.1};
GN ORFNames=HHUB_3057 {ECO:0000313|EMBL:CQH59774.1};
OS Halobacterium hubeiense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=1407499 {ECO:0000313|EMBL:CQH59774.1, ECO:0000313|Proteomes:UP000066737};
RN [1] {ECO:0000313|Proteomes:UP000066737}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JI20-1 {ECO:0000313|Proteomes:UP000066737};
RX PubMed=26628271; DOI=10.1111/1462-2920.13130;
RA Jaakkola S.T., Pfeiffer F., Ravantti J.J., Guo Q., Liu Y., Chen X., Ma H.,
RA Yang C., Oksanen H.M., Bamford D.H.;
RT "The complete genome of a viable archaeum isolated from 123-million-year-
RT old rock salt.";
RL Environ. Microbiol. 18:565-579(2016).
CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-
CC hydroxy-4-methylpentanoate (2-isopropylmalate).
CC {ECO:0000256|ARBA:ARBA00003715}.
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}.
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DR EMBL; LN831302; CQH59774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5H4U4; -.
DR STRING; 1407499.HHUB_3057; -.
DR KEGG; hhb:Hhub_3057; -.
DR OrthoDB; 6555at2157; -.
DR Proteomes; UP000066737; Chromosome I.
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:CQH59774.1};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Reference proteome {ECO:0000313|Proteomes:UP000066737};
KW Transferase {ECO:0000256|RuleBase:RU003523, ECO:0000313|EMBL:CQH59774.1}.
FT DOMAIN 22..272
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 399 AA; 42280 MW; E0E27DDFA6E1FD39 CRC64;
MQVRGNEFFQ GTLAQRNEFD TVRIFDTTLR DGEQTPRTSF SYDDKRAIAA ALDDANVDVI
EAGFPANSEQ EAEAVADIAA STDATTCGLA RVVESDVEAA IDAGVGMIHV FASTSDVQIE
DSMHSTREDV VARSVAAVEQ AAASGAEVMF SPMDATRTDP QFLAEIVEAV DEVGVDWINI
PDTCGVGTPK RFGELVEYVG QHTDARIDVH THDDFGLATA NALTGVEYGA DQMQVSVNGI
GERAGNAAFE EVVMAAESLY GADTGVDTTA ITDLSKLVSE RSSVPVPVNK PVVGAHAFAH
ESGIHAAGVI ENSETFEPGV MTPEMVGAER EVVLGKHTGT HAVRDHLEDA GFAPTDEEVR
EVTKKVKAHA GDDEVVTDAV LRAFAGEVGI DRETEEVTA
//
