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Database: UniProt
Entry: C1G792_PARBD
LinkDB: C1G792_PARBD
Original site: C1G792_PARBD 
ID   C1G792_PARBD            Unreviewed;       562 AA.
AC   C1G792;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 60.
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   ORFNames=PADG_03047 {ECO:0000313|EMBL:EEH46949.1};
OS   Paracoccidioides brasiliensis (strain Pb18).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH46949.1, ECO:0000313|Proteomes:UP000001628};
RN   [1] {ECO:0000313|EMBL:EEH46949.1, ECO:0000313|Proteomes:UP000001628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb18 {ECO:0000313|EMBL:EEH46949.1,
RC   ECO:0000313|Proteomes:UP000001628};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108,
CC         ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19;
CC         Evidence={ECO:0000256|ARBA:ARBA00001274,
CC         ECO:0000256|RuleBase:RU362012};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU362012};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from L-threonine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004810, ECO:0000256|RuleBase:RU362012}.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       {ECO:0000256|ARBA:ARBA00010869, ECO:0000256|RuleBase:RU362012}.
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DR   EMBL; KN275959; EEH46949.1; -; Genomic_DNA.
DR   RefSeq; XP_010758700.1; XM_010760398.1.
DR   AlphaFoldDB; C1G792; -.
DR   STRING; 502780.C1G792; -.
DR   GeneID; 22582419; -.
DR   KEGG; pbn:PADG_03047; -.
DR   VEuPathDB; FungiDB:PADG_03047; -.
DR   eggNOG; KOG1250; Eukaryota.
DR   HOGENOM; CLU_021152_6_0_1; -.
DR   InParanoid; C1G792; -.
DR   OMA; VNFPQRA; -.
DR   OrthoDB; 5476420at2759; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000001628; Unassembled WGS sequence.
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   CDD; cd04906; ACT_ThrD-I_1; 1.
DR   CDD; cd04907; ACT_ThrD-I_2; 1.
DR   CDD; cd01562; Thr-dehyd; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR045865; ACT-like_dom_sf.
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; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01124; ilvA_2Cterm; 1.
DR   PANTHER; PTHR48078:SF11; THREONINE DEHYDRATASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF00585; Thr_dehydrat_C; 2.
DR   SUPFAM; SSF55021; ACT-like; 2.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS51672; ACT_LIKE; 2.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU362012};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|RuleBase:RU362012};
KW   Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624,
KW   ECO:0000256|RuleBase:RU362012};
KW   Lyase {ECO:0000256|RuleBase:RU362012, ECO:0000313|EMBL:EEH46949.1};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU362012};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          385..459
FT                   /note="ACT-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51672"
FT   DOMAIN          481..552
FT                   /note="ACT-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51672"
SQ   SEQUENCE   562 AA;  61464 MW;  03FB61A6CF5CFF04 CRC64;
     MAETPLTNGN GSPRTPRLNS LALTEGSAKT TTSNERHGPS ADWDIPEAYL LPNGYPDYLR
     LILTSRVYDV VQETPLTHAV NMSNRLECKV LLKREDLLPV FSFKLRGAYN KMAHLSPERM
     WKGVIACSAG NHAQGVAYSA RTLKIPATIV MPSGTPAIKH RNVARLGGTV VLHGPDFDSA
     KMEAARLAKL YDLTNIPPFD DPYVIAGQGT CGMELLRQSN LQNLEAVFCC VGGGGLIAGV
     GVYIKRIAPH VKIIGVETHD ANAMARSLTD GERVTLKEVG LFADGAAVKA VGEETFRLCR
     EVVDDIIQVS TDEACAAIKD VFEDTRSIME PAGALALAGL KKYVAMNPSP NPNRELVAIT
     SGANMNFDRL RFVAERATLG ERKEALLSVT VPERPGAFAK LIELVTPLDV TELSYRYSCP
     ESANLFIGLS LSSPTGTDDL SHITRQLLAC GMIASDLSDD ELAKTHIRYL GGGRSNVAEE
     RLFMFEFPER PGALMKFLRT LKPHQNISLF HYRNYGSDVA KVLAGIQCPA AEKRELEDFL
     HDLGYPFIEC THSPVYKTFL RE
//
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