(data stored in SCRATCH zone)

SWISSPROT: C8W663_DESAS

ID   C8W663_DESAS            Unreviewed;       521 AA.
AC   C8W663;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   SubName: Full=2-isopropylmalate synthase/homocitrate synthase family protein {ECO:0000313|EMBL:ACV61518.1};
GN   OrderedLocusNames=Dtox_0598 {ECO:0000313|EMBL:ACV61518.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61518.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61518.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000256|RuleBase:RU003523,
CC       ECO:0000256|SAAS:SAAS00580399}.
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DR   EMBL; CP001720; ACV61518.1; -; Genomic_DNA.
DR   RefSeq; WP_015756237.1; NC_013216.1.
DR   STRING; 485916.Dtox_0598; -.
DR   EnsemblBacteria; ACV61518; ACV61518; Dtox_0598.
DR   KEGG; dae:Dtox_0598; -.
DR   eggNOG; ENOG4105CYQ; Bacteria.
DR   eggNOG; COG0119; LUCA.
DR   HOGENOM; HOG000046860; -.
DR   KO; K01649; -.
DR   OMA; KSWDFHV; -.
DR   OrthoDB; 840579at2; -.
DR   BioCyc; DACE485916:G1GFV-604-MONOMER; -.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005675; Citramal_synthase.
DR   InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR   InterPro; IPR000891; PYR_CT.
DR   PANTHER; PTHR43538; PTHR43538; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF08502; LeuA_dimer; 1.
DR   SMART; SM00917; LeuA_dimer; 1.
DR   SUPFAM; SSF110921; SSF110921; 1.
DR   TIGRFAMs; TIGR00977; citramal_synth; 1.
DR   PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8W663.
DR   SWISS-2DPAGE; C8W663.
KW   Amino-acid biosynthesis {ECO:0000256|SAAS:SAAS00161459};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|SAAS:SAAS00160591}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Transferase {ECO:0000256|RuleBase:RU003523,
KW   ECO:0000256|SAAS:SAAS00131367}.
FT   DOMAIN        4    269       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
FT   COILED      349    369       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   521 AA;  57250 MW;  3639710EFC26ED30 CRC64;
     MSTIEIYDTT LRDGAQGEGI SFSVEDKVKI ALRLDKLGVH YIEGGWPGSN PKDSDFFKRI
     KDFPLEKAVV SAFGSTRKPN SDVKEDVNLK AIVDAGVQVA CIFGKTWDFQ VVYALNTTLE
     ENLQMIKESV AYLKSNGMQV FYDAEHFFDG CKANTEYALE TVKAAQAGGA DRIVLCDTNG
     GTMPWDIQEI VSKVKSVVTV PLGIHCHNDS EMAAANSVIA VQSGVIQVQG TMNGYGERCG
     NANLCSVIPN LEIKCGLKCL PEGNLAQLTE VSRFVSEVAN MHLHNGQPFV GTSAFAHKGG
     IHVSAIMKNS KTYEHITPEL VGNQRRVLVS DQSGLSNLLY KFKELNVDLT QQTEENKQLL
     MHIKELENQG YQFEGADGSF ELLMRRISGQ YENPFKLESL RVIMDMKENG PTSTEATIKI
     WVGDQVKHTA AEGNGPVNAL DNALRKSLEG FYPAIKEMQL NDYKVRVLNE KEGTDAVVRV
     SIETGDGKNS WGTIGVSTNI MEASWQALVD SLAYGLLKQN D
//

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