(data stored in SCRATCH zone)

SWISSPROT: A0LEA9_SYNFM

ID   A0LEA9_SYNFM            Unreviewed;       434 AA.
AC   A0LEA9;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 81.
DE   RecName: Full=Diaminopimelate decarboxylase {ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};
DE            Short=DAP decarboxylase {ECO:0000256|HAMAP-Rule:MF_02120};
DE            Short=DAPDC {ECO:0000256|HAMAP-Rule:MF_02120};
DE            EC=4.1.1.20 {ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};
GN   Name=lysA {ECO:0000256|HAMAP-Rule:MF_02120};
GN   OrderedLocusNames=Sfum_0058 {ECO:0000313|EMBL:ABK15761.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK15761.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK15761.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically catalyzes the decarboxylation of meso-
CC       diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-
CC       Rule:MF_02120}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + meso-2,6-diaminopimelate = CO2 + L-lysine;
CC         Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02120,
CC         ECO:0000256|RuleBase:RU003738};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02120,
CC         ECO:0000256|RuleBase:RU003738, ECO:0000256|SAAS:SAAS00373528};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02120}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
CC       family. LysA subfamily. {ECO:0000256|HAMAP-Rule:MF_02120}.
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DR   EMBL; CP000478; ABK15761.1; -; Genomic_DNA.
DR   STRING; 335543.Sfum_0058; -.
DR   EnsemblBacteria; ABK15761; ABK15761; Sfum_0058.
DR   KEGG; sfu:Sfum_0058; -.
DR   eggNOG; ENOG4105CU5; Bacteria.
DR   eggNOG; COG0019; LUCA.
DR   HOGENOM; HOG000045070; -.
DR   KO; K01586; -.
DR   OMA; HGNAKSP; -.
DR   UniPathway; UPA00034; UER00027.
DR   Proteomes; UP000001784; Chromosome.
DR   GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR   CDD; cd06828; PLPDE_III_DapDC; 1.
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; IPR022657; De-COase2_CS.
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.
DR   TIGRFAMs; TIGR01048; lysA; 1.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0LEA9.
DR   SWISS-2DPAGE; A0LEA9.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02120};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_02120,
KW   ECO:0000256|RuleBase:RU003738};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738,
KW   ECO:0000313|EMBL:ABK15761.1};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02120,
KW   ECO:0000256|RuleBase:RU003738};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02120,
KW   ECO:0000256|SAAS:SAAS00272807};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784}.
FT   DOMAIN       39    379       Orn_DAP_Arg_deC. {ECO:0000259|Pfam:
FT                                PF00278}.
FT   DOMAIN       48    289       Orn_Arg_deC_N. {ECO:0000259|Pfam:
FT                                PF02784}.
FT   REGION      283    286       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_02120}.
FT   BINDING     249    249       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02120}.
FT   BINDING     286    286       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   BINDING     322    322       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   BINDING     326    326       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   BINDING     353    353       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   BINDING     381    381       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_02120}.
FT   BINDING     381    381       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   MOD_RES      70     70       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02120}.
SQ   SEQUENCE   434 AA;  48244 MW;  D4750D01FFB15014 CRC64;
     MTGSADRGFL MHHFHYHNDE LYCERVPLRE LAARVGTPCY VYSHATLLHH FTVFDSAFEG
     VPHLTCFSVK ANSNLAVLRL FGSLGGGVDI VSGGELYRAR QAGIAPDKIV YSGVGKTLEE
     IDYALRENIL MFNIESTQEL EAINARAAAF GCRARIALRV NPDVDPNTHP YISTGMKKNK
     FGIEIDSAVK AYERARSLDH VEVVGVDCHI GSQLTEISPF VDALKRLRLL IEKLEAVGIT
     IQYLDLGGGL GIVYDQEAPP EPREYARAIL RELKGMHCTL IFEPGRVIVG NAGVLLARVL
     YTKRTQSKSF IITDTAMNDL IRPSLYGSYH QVQPLRRQSR ESHIVDVVGP ICESGDFIAK
     DRGLPMVESG DFLAVMSAGA YGFTMSSNYN SRPRAAEVLV KDDRYFVIRR RETWDDLIQC
     ETIPAFLSSD KQPA
//

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