ID C7NVR1_HALMD Unreviewed; 515 AA.
AC C7NVR1;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Pyruvate carboxyltransferase {ECO:0000313|EMBL:ACV46176.1};
GN OrderedLocusNames=Hmuk_0025 {ECO:0000313|EMBL:ACV46176.1};
OS Halomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB
OS 13541) (Haloarcula mukohataei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halomicrobium.
OX NCBI_TaxID=485914 {ECO:0000313|EMBL:ACV46176.1, ECO:0000313|Proteomes:UP000001746};
RN [1] {ECO:0000313|EMBL:ACV46176.1, ECO:0000313|Proteomes:UP000001746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541
RC {ECO:0000313|Proteomes:UP000001746};
RX PubMed=21304667; DOI=10.4056/sigs.42644;
RA Tindall B.J., Schneider S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA Goodwin L., Pitluck S., Mikhailova N., Pati A., Ivanova N., Mavrommatis K.,
RA Chen A., Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Han C., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.,
RA Detter J.C.;
RT "Complete genome sequence of Halomicrobium mukohataei type strain (arg-
RT 2).";
RL Stand. Genomic Sci. 1:270-277(2009).
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|ARBA:ARBA00006154, ECO:0000256|RuleBase:RU003523}.
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DR EMBL; CP001688; ACV46176.1; -; Genomic_DNA.
DR AlphaFoldDB; C7NVR1; -.
DR STRING; 485914.Hmuk_0025; -.
DR KEGG; hmu:Hmuk_0025; -.
DR eggNOG; arCOG02092; Archaea.
DR HOGENOM; CLU_022158_0_1_2; -.
DR Proteomes; UP000001746; Chromosome.
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; 3.30.160.270; -; 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; PTHR42880:SF2; (R)-CITRAMALATE SYNTHASE CIMA; 1.
DR PANTHER; PTHR42880; HOMOCITRATE SYNTHASE; 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:ARBA00023304};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Pyruvate {ECO:0000313|EMBL:ACV46176.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001746};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 22..270
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 515 AA; 54239 MW; 70F18030298F9857 CRC64;
MTETTLFGGH PLTRDLSDAD GVQFLDTTLR DGEQAPGISL SPDEKARIAR QLDAAEIDVI
EAGSACTGPG ERKTISRVAD LDLDATVTSF CRGIRNDIDL ALECGVDGIN LVVPASDRHV
EDKVGTSRED NVASTVELVE YAKAQGLWVE VIGEDGSRAD LDYLEELLGA AIDAGADRIC
WADTVGHATP DGALEAVSRL SKLGPVSAHT HDDLGLAVMN ALVAVAAGAD MVHGTINGIG
ERAGNVALEE VAIALDHGYG VETMDLTEVY DLAQLVANTT GIQLAPNKAV VGQNAFTHES
GIHTDGTLKD DAMYEPYRPE KVGRERRLAL GKHAGRAGVA AALDEHDIDV SDDELATIVG
RVKEIGDRGR RVTDADLLTI AEEVKGTDRE RRVELLDLTT IAGGGTPTAS IRLAVDGEER
EPASATGSGP VDAAMTAIEE ALGSSVNWNL DSYHVDAITG NTDAVVTVEV EMSRGDRTVT
VSNSDSDITR ASVHAMVDAI DRLLADEDEP VVADD
//
