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Database: UniProt
Entry: Q980Z1_SACS2
LinkDB: Q980Z1_SACS2
Original site: Q980Z1_SACS2 
ID   Q980Z1_SACS2            Unreviewed;       553 AA.
AC   Q980Z1;
DT   01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2001, sequence version 1.
DT   08-NOV-2023, entry version 110.
DE   RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE            EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN   Name=leuA-1 {ECO:0000313|EMBL:AAK40481.1};
GN   OrderedLocusNames=SSO0127 {ECO:0000313|EMBL:AAK40481.1};
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057 {ECO:0000313|EMBL:AAK40481.1, ECO:0000313|Proteomes:UP000001974};
RN   [1] {ECO:0000313|Proteomes:UP000001974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2
RC   {ECO:0000313|Proteomes:UP000001974};
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from pyruvate: step 1/3. {ECO:0000256|ARBA:ARBA00004743}.
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; AE006641; AAK40481.1; -; Genomic_DNA.
DR   PIR; B90153; B90153.
DR   AlphaFoldDB; Q980Z1; -.
DR   STRING; 273057.SSO0127; -.
DR   PaxDb; 273057-SSO0127; -.
DR   EnsemblBacteria; AAK40481; AAK40481; SSO0127.
DR   KEGG; sso:SSO0127; -.
DR   PATRIC; fig|273057.12.peg.122; -.
DR   eggNOG; arCOG02092; Archaea.
DR   HOGENOM; CLU_022158_7_0_2; -.
DR   InParanoid; Q980Z1; -.
DR   OMA; KSWDFHV; -.
DR   PhylomeDB; Q980Z1; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR   CDD; cd07941; DRE_TIM_LeuA3; 1.
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; IPR005675; Citramal_synthase.
DR   InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR   InterPro; IPR000891; PYR_CT.
DR   NCBIfam; TIGR00977; citramal_synth; 1.
DR   PANTHER; PTHR43538:SF1; (R)-CITRAMALATE SYNTHASE; 1.
DR   PANTHER; PTHR43538; ALPHA-IPM SYNTHASE/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; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW   Lyase {ECO:0000313|EMBL:AAK40481.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001974};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          33..296
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   553 AA;  61264 MW;  DC6194F7B6D22282 CRC64;
     MALKMKYDFL LLSLKLLNLP IIFHLCSVSK KSVEVLDTTL RDGSQGANIS FTLNDKIKIA
     LLLDELGVDY IEGGWPGSNP KDEEFFREIK KYRLSKAKIA AFGSTKRKDV SVKEDISLNS
     IVKADVDVAV IFGKSWSLHA TEVLKVTKQD NLDIVYDSIN YLKSHGLKVI FDAEHFYQGF
     KEDPEYALEV VKTAESAGAD VIALADTNGG TPPFEVYEIT KKVREVLQVK LGIHAHNDIG
     CAVANSLMAI KAGARHVQGT INGIGERTGN ADLIQIIPTL ILKMGLNALN GQESLRKLRE
     VSRIVYEILG LPPNPYQPYV GDNAFAHKAG VHVDAVMKVP RAYEHVDPSL VGNDRKFVIS
     ELSGTANLVS YLQGLGIAVD KKDERLKKAL NKIKELEARG YSFDVGPASA ILITLKELNI
     YKNYINLEYW KVINENNGLS IGIVKVNSQL EVAEGVGPVN AIDRALRMAL QRVYPEIGEV
     KLIDYRVILP SEIKNTESVV RVTIEFTDNK MNWRTEGVSK SVVEASVMAL VDGLDYYLQL
     KKTLKTAVDN YIV
//
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