(data stored in SCRATCH zone)

SWISSPROT: C5DCQ0_LACTC

ID   C5DCQ0_LACTC            Unreviewed;       573 AA.
AC   C5DCQ0;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   16-JAN-2019, entry version 54.
DE   RecName: Full=Threonine dehydratase {ECO:0000256|RuleBase:RU362012};
DE            EC=4.3.1.19 {ECO:0000256|RuleBase:RU362012};
DE   AltName: Full=Threonine deaminase {ECO:0000256|RuleBase:RU362012};
GN   OrderedLocusNames=KLTH0B04884g {ECO:0000313|EMBL:CAR21561.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21561.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21561.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine = 2-oxobutanoate + NH4(+);
CC         Xref=Rhea:RHEA:22108, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57926; EC=4.3.1.19;
CC         Evidence={ECO:0000256|RuleBase:RU362012};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU362012};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from L-threonine: step 1/1.
CC       {ECO:0000256|RuleBase:RU362012}.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       {ECO:0000256|RuleBase:RU362012}.
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DR   EMBL; CU928166; CAR21561.1; -; Genomic_DNA.
DR   RefSeq; XP_002551999.1; XM_002551953.1.
DR   STRING; 381046.XP_002551999.1; -.
DR   EnsemblFungi; CAR21561; CAR21561; KLTH0B04884g.
DR   GeneID; 8290837; -.
DR   KEGG; lth:KLTH0B04884g; -.
DR   HOGENOM; HOG000046975; -.
DR   InParanoid; C5DCQ0; -.
DR   KO; K01754; -.
DR   OMA; RNHGAAY; -.
DR   OrthoDB; 906802at2759; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000002036; Chromosome B.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1020.10; -; 1.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR001721; TD_ACT-like.
DR   InterPro; IPR038110; TD_ACT-like_sf.
DR   InterPro; IPR005787; Thr_deHydtase_biosynth.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF00585; Thr_dehydrat_C; 2.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR01124; ilvA_2Cterm; 1.
DR   PROSITE; PS51672; ACT_LIKE; 2.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5DCQ0.
DR   SWISS-2DPAGE; C5DCQ0.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU362012};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|RuleBase:RU362012};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW   Isoleucine biosynthesis {ECO:0000256|RuleBase:RU362012};
KW   Lyase {ECO:0000256|RuleBase:RU362012};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU362012};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036}.
FT   DOMAIN      390    470       ACT-like. {ECO:0000259|PROSITE:PS51672}.
FT   DOMAIN      492    563       ACT-like. {ECO:0000259|PROSITE:PS51672}.
SQ   SEQUENCE   573 AA;  63199 MW;  0F7523E083E3CE04 CRC64;
     MASKISSQEL KMSSTLLTRT RPALVSRFLL RYQSSAVANL QKLHAKLNPD ELLPDSTPDY
     VRLILRSSVY DVIEESPITR GVGLSSRLNT NVQLKREDLL PVFSFKLRGA YNMMAKLSEA
     QKNQGVIACS AGNHAQGVAF ASRHLNIPAI IVMPVNTPSI KYQNVSRLGG QVVLYGNDFD
     EAKTECTRIS EERGLTNIPP FDHPYVIAGQ GTVAMEILRQ VHNAAKIGAV FVPVGGGGLV
     AGVAAYLKRI APHIKIIGVE TYDSATLKTS LEAGTRTPLS TVGTFADGTS VRMIGEETFR
     ICQDLVDDVI LVNTDEICAA VKDIFEDTRS IVEPSGALAV AGLKKYVTQV HPDVDHSKKT
     YVPILSGANM NFDRLRFVSE RAVLGEGKEV FMLVTIPDVP GSFKQLQRVI HPRAVTEFSY
     RYNEHRHSSA SDVPKAYIYT SFSVVDREKE IKQVLQQLHG LGFDAVDISD NEMAKSHGRY
     LVGGASKVPN EKIVSFEFPE RPGALTKFLD GMSDSWNLTL FHYRNHGSDV GKVLAGVSVS
     AEDNEGFQKF LDDLGYKYQD ETNNMVYQKF LKF
//

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