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Database: UniProt
Entry: Q9HK20
LinkDB: Q9HK20
Original site: Q9HK20 
ID   DCDA_THEAC              Reviewed;         402 AA.
AC   Q9HK20;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   01-OCT-2014, entry version 71.
DE   RecName: Full=Diaminopimelate decarboxylase {ECO:0000255|HAMAP-Rule:MF_02120};
DE            Short=DAP decarboxylase {ECO:0000255|HAMAP-Rule:MF_02120};
DE            Short=DAPDC {ECO:0000255|HAMAP-Rule:MF_02120};
DE            EC=4.1.1.20 {ECO:0000255|HAMAP-Rule:MF_02120};
GN   Name=lysA {ECO:0000255|HAMAP-Rule:MF_02120}; OrderedLocusNames=Ta0788;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 /
OS   NBRC 15155 / AMRC-C165).
OC   Archaea; Euryarchaeota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
CC   -!- FUNCTION: Specifically catalyzes the decarboxylation of meso-
CC       diaminopimelate (meso-DAP) to L-lysine. {ECO:0000255|HAMAP-
CC       Rule:MF_02120}.
CC   -!- CATALYTIC ACTIVITY: Meso-2,6-diaminoheptanedioate = L-lysine +
CC       CO(2). {ECO:0000255|HAMAP-Rule:MF_02120}.
CC   -!- COFACTOR: Pyridoxal phosphate. {ECO:0000255|HAMAP-Rule:MF_02120}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_02120}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02120}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
CC       family. LysA subfamily. {ECO:0000255|HAMAP-Rule:MF_02120}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC11919.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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DR   EMBL; AL445065; CAC11919.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_394250.1; NC_002578.1.
DR   ProteinModelPortal; Q9HK20; -.
DR   STRING; 273075.Ta0788m; -.
DR   EnsemblBacteria; CAC11919; CAC11919; CAC11919.
DR   GeneID; 1457041; -.
DR   KEGG; tac:Ta0788m; -.
DR   eggNOG; COG0019; -.
DR   KO; K01586; -.
DR   UniPathway; UPA00034; UER00027.
DR   GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_02120; LysA; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR002986; DAP_deCOOHase_LysA.
DR   InterPro; IPR022643; De-COase2_C.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR   PRINTS; PR01181; DAPDCRBXLASE.
DR   PRINTS; PR01179; ODADCRBXLASE.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Decarboxylase; Lyase;
KW   Lysine biosynthesis; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    402       Diaminopimelate decarboxylase.
FT                                /FTId=PRO_0000411132.
FT   REGION      269    272       Pyridoxal phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_02120}.
FT   BINDING     233    233       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_02120}.
FT   BINDING     272    272       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_02120}.
FT   BINDING     304    304       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_02120}.
FT   BINDING     308    308       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_02120}.
FT   BINDING     334    334       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_02120}.
FT   BINDING     360    360       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_02120}.
FT   BINDING     360    360       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_02120}.
FT   MOD_RES      61     61       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_02120}.
SQ   SEQUENCE   402 AA;  44844 MW;  6944F0C283619C03 CRC64;
     MGIYDIFDDE SARSISGMSI DEMAKKYGTP VIIYSRARIV SNIRRIREAY ENRVRMLYSV
     KANDNPRIIE IMHQESIGSD SASPMEIMMS IFSGIPPEDI LYSPNNASEY DLNFALDRGI
     AINFNTFTQY RKMREKPERI SFRINPGFGM GEFAGTTTGG ARTKFGIDPD AAILAYRKAR
     EDGIREFGIH MMIGSNNRDH VKIAEAYSNF FRIADRIGRE AGVSFQFADV GGGLGIPYVQ
     GENELDIAAL GSAVLKEFDR YHFGDLVLEP GRYLVGDAGI IVGTVNDVHN GFAGTDIGMN
     LNIRPALYGA RHTIIPVGER VEGEKITVTG QICENTDRIG DTAWRLSEGD RIMVLDAGAY
     VYSMSSRYNG RPRPPEIMIM EDGKDVMIRR REDFSDFIAT VV
//
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