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Database: UniProt/TrEMBL
Entry: D3DFE6_HYDTT
LinkDB: D3DFE6_HYDTT
Original site: D3DFE6_HYDTT 
ID   D3DFE6_HYDTT            Unreviewed;       415 AA.
AC   D3DFE6;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   19-MAR-2014, entry version 33.
DE   RecName: Full=Diaminopimelate decarboxylase;
DE            Short=DAP decarboxylase;
DE            Short=DAPDC;
DE            EC=4.1.1.20;
GN   Name=lysA; OrderedLocusNames=HTH_0081, Hydth_0082;
OS   Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobacter.
OX   NCBI_TaxID=608538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6534 / IAM 12695 / TK-6 [Tokyo], and TK-6;
RX   PubMed=20348262; DOI=10.1128/JB.00158-10;
RA   Arai H., Kanbe H., Ishii M., Igarashi Y.;
RT   "Complete genome sequence of the thermophilic, obligately
RT   chemolithoautotrophic hydrogen-oxidizing bacterium Hydrogenobacter
RT   thermophilus TK-6.";
RL   J. Bacteriol. 192:2651-2652(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6534 / IAM 12695 / TK-6 [JGI], and TK-6;
RX   DOI=10.4056/sigs.1463589;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Zeytun A., Sikorski J., Nolan M., Lapidus A., Lucas S., Han J.,
RA   Tice H., Cheng J., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A.,
RA   Chen A., Palaniappan K., Ngatchou O., Land M., Hauser L., Chang Y.,
RA   Jeffries C., Han C., Detter J., Ubler S., Rohde M., Tindall B.,
RA   Wirth R., Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Klenk H., Kyrpides N.;
RT   "Complete genome sequence of Hydrogenobacter thermophilus type strain
RT   (TK-6).";
RL   Stand. Genomic Sci. 4:131-143(2011).
CC   -!- FUNCTION: Specifically catalyzes the decarboxylation of meso-
CC       diaminopimelate (meso-DAP) to L-lysine (By similarity).
CC   -!- CATALYTIC ACTIVITY: Meso-2,6-diaminoheptanedioate = L-lysine +
CC       CO(2).
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
CC       family. LysA subfamily.
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DR   EMBL; CP002221; ADO44492.1; -; Genomic_DNA.
DR   EMBL; AP011112; BAI68548.1; -; Genomic_DNA.
DR   RefSeq; YP_003431749.1; NC_013799.1.
DR   RefSeq; YP_005510785.1; NC_017161.1.
DR   EnsemblBacteria; ADO44492; ADO44492; Hydth_0082.
DR   EnsemblBacteria; BAI68548; BAI68548; HTH_0081.
DR   GeneID; 12101246; -.
DR   GeneID; 8772074; -.
DR   KEGG; hte:Hydth_0082; -.
DR   KEGG; hth:HTH_0081; -.
DR   PATRIC; 32209021; VBIHydThe36152_0082.
DR   HOGENOM; HOG000045070; -.
DR   KO; K01586; -.
DR   OMA; NKFGIPI; -.
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   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; IPR022657; De-COase2_CS.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR   InterPro; IPR000183; Orn/DAP/Arg_de-COase.
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   TIGRFAMs; TIGR01048; lysA; 1.
DR   PROSITE; PS00878; ODR_DC_2_1; 1.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Decarboxylase; Lyase;
KW   Lysine biosynthesis; Pyridoxal phosphate.
FT   REGION      277    280       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING     242    242       Pyridoxal phosphate; via amide nitrogen
FT                                (By similarity).
FT   BINDING     280    280       Substrate (By similarity).
FT   BINDING     316    316       Substrate (By similarity).
FT   BINDING     320    320       Substrate (By similarity).
FT   BINDING     347    347       Substrate (By similarity).
FT   BINDING     375    375       Pyridoxal phosphate (By similarity).
FT   BINDING     375    375       Substrate (By similarity).
FT   MOD_RES      63     63       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   415 AA;  46385 MW;  96AE79409D03DE61 CRC64;
     MLKEYNRYLE YIDGELHLEG VSLKALAEEF GTPLYVYSAS HIRDRVRAYR EAFPDALICY
     AVKANFNPSI IRVAREEGAG ADIVSGGELY ASLLAGVEPS RIVYAGVGKT LKELEYAIKS
     DILMFNVESR MELDVLNHLA ESLGKKIRIA IRVNPDVDPK THPYISTGMK KSKFGVDIKH
     AKQEYQYAGK LKNLEVVGIH CHIGSQILDV SPYIEAVEKV VDLYHELVRS GFEIRYVDIG
     GGLGIKYKPD QSNPEPKDLA EAVMPALKGV DAKILLEPGR SIVGNAGLLI TRVEFLKDKG
     HKHFVIVDAG MNDLIRPAMY DAYHHIVPVV KRDTGYIKTD IVGPICETGD FLALDREIQK
     VERGDYLAVL SAGAYGFAMS SHYNVRPRAC EVLVEKQSYK IIRERETYAY IFKGE
//
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