(data stored in ACNUC7421 zone)

SWISSPROT: Q13IG7_PARXL

ID   Q13IG7_PARXL            Unreviewed;       203 AA.
AC   Q13IG7;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 79.
DE   RecName: Full=D-alanyl-D-alanine dipeptidase {ECO:0000256|HAMAP-Rule:MF_01924, ECO:0000256|PIRNR:PIRNR026671};
DE            Short=D-Ala-D-Ala dipeptidase {ECO:0000256|HAMAP-Rule:MF_01924, ECO:0000256|PIRNR:PIRNR026671};
DE            EC=3.4.13.22 {ECO:0000256|HAMAP-Rule:MF_01924, ECO:0000256|PIRNR:PIRNR026671};
GN   Name=ddpX {ECO:0000256|HAMAP-Rule:MF_01924};
GN   ORFNames=Bxe_C0198 {ECO:0000313|EMBL:ABE36122.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36122.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE36122.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE36122.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Catalyzes hydrolysis of the D-alanyl-D-alanine
CC       dipeptide. {ECO:0000256|HAMAP-Rule:MF_01924,
CC       ECO:0000256|PIRNR:PIRNR026671}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-alanyl-D-alanine + H2O = 2 D-alanine;
CC         Xref=Rhea:RHEA:20661, ChEBI:CHEBI:15377, ChEBI:CHEBI:57416,
CC         ChEBI:CHEBI:57822; EC=3.4.13.22; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01924, ECO:0000256|PIRNR:PIRNR026671};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01924};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01924};
CC   -!- SIMILARITY: Belongs to the peptidase M15D family.
CC       {ECO:0000256|HAMAP-Rule:MF_01924, ECO:0000256|PIRNR:PIRNR026671}.
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DR   EMBL; CP000272; ABE36122.1; -; Genomic_DNA.
DR   STRING; 266265.Bxe_C0198; -.
DR   MEROPS; M15.011; -.
DR   EnsemblBacteria; ABE36122; ABE36122; Bxe_C0198.
DR   KEGG; bxe:Bxe_C0198; -.
DR   eggNOG; ENOG4108UQS; Bacteria.
DR   eggNOG; COG2173; LUCA.
DR   HOGENOM; HOG000200848; -.
DR   KO; K08641; -.
DR   Proteomes; UP000001817; Chromosome 3.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1380.10; -; 1.
DR   HAMAP; MF_01924; A_A_dipeptidase; 1.
DR   InterPro; IPR000755; A_A_dipeptidase.
DR   InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR   Pfam; PF01427; Peptidase_M15; 1.
DR   PIRSF; PIRSF026671; AA_dipeptidase; 1.
DR   SUPFAM; SSF55166; SSF55166; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13IG7.
DR   SWISS-2DPAGE; Q13IG7.
KW   Cell wall biogenesis/degradation {ECO:0000256|PIRNR:PIRNR026671};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Dipeptidase {ECO:0000256|HAMAP-Rule:MF_01924,
KW   ECO:0000256|PIRNR:PIRNR026671, ECO:0000313|EMBL:ABE36122.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01924,
KW   ECO:0000256|PIRNR:PIRNR026671, ECO:0000313|EMBL:ABE36122.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01924};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_01924,
KW   ECO:0000256|PIRNR:PIRNR026671};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_01924,
KW   ECO:0000256|PIRNR:PIRNR026671};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01924}.
FT   ACT_SITE    177    177       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_01924}.
FT   METAL       113    113       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01924}.
FT   METAL       120    120       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01924}.
FT   METAL       180    180       Zinc; via pros nitrogen; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01924}.
FT   SITE         86     86       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01924}.
SQ   SEQUENCE   203 AA;  22330 MW;  7A8BB9B70CE59BF8 CRC64;
     MRSLSPLSSG HPTAPSMTKS RLIEITPATH GVDIDLVYAT GRNLTGKPIY KEAHCLLLEP
     AEAGLRNAIG IARDAGLRLR IFDAYRPPQA QQVLWDFLPD STYVAEPERG SNHSRGTAID
     LTLLDAGGHE LDMGTGFDAM TIESEHFHPG LPVHVQRNRL LLLGIMHAAG FAHIKNEWWH
     YELPGSRALP LIDDSESGTL RLM
//

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