ID A0A8A6KHP7_9PROT Unreviewed; 182 AA. AC A0A8A6KHP7; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 19-JAN-2022, entry version 2. DE RecName: Full=D-alanyl-D-alanine dipeptidase {ECO:0000256|HAMAP-Rule:MF_01924}; DE Short=D-Ala-D-Ala dipeptidase {ECO:0000256|HAMAP-Rule:MF_01924}; DE EC=3.4.13.22 {ECO:0000256|HAMAP-Rule:MF_01924}; GN Name=ddpX {ECO:0000256|HAMAP-Rule:MF_01924, GN ECO:0000313|EMBL:QTI79349.1}; GN ORFNames=IAI58_00465 {ECO:0000313|EMBL:QTI79349.1}; OS Roseomonas sp. 1318. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Roseomonas; unclassified Roseomonas. OX NCBI_TaxID=2768161 {ECO:0000313|EMBL:QTI79349.1}; RN [1] {ECO:0000313|EMBL:QTI79349.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1318 {ECO:0000313|EMBL:QTI79349.1}; RA Wang C., Li S., Zhu W.; RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide. CC {ECO:0000256|HAMAP-Rule:MF_01924}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-alanyl-D-alanine + H2O = 2 D-alanine; Xref=Rhea:RHEA:20661, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57416, ChEBI:CHEBI:57822; CC EC=3.4.13.22; Evidence={ECO:0000256|ARBA:ARBA00001362, CC ECO:0000256|HAMAP-Rule:MF_01924}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01924}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01924}; CC -!- SIMILARITY: Belongs to the peptidase M15D family. {ECO:0000256|HAMAP- CC Rule:MF_01924}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP061091; QTI79349.1; -; Genomic_DNA. DR GO; GO:0016805; F:dipeptidase activity; 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; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316}; KW Dipeptidase {ECO:0000256|HAMAP-Rule:MF_01924, ECO:0000313|EMBL:QTI79349.1}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01924, ECO:0000313|EMBL:QTI79349.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01924}; KW Metalloprotease {ECO:0000256|HAMAP-Rule:MF_01924}; KW Protease {ECO:0000256|HAMAP-Rule:MF_01924}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01924}. FT ACT_SITE 157 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924" FT METAL 92 FT /note="Zinc; via tele nitrogen; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924" FT METAL 99 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924" FT METAL 160 FT /note="Zinc; via pros nitrogen; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924" FT SITE 65 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924" SQ SEQUENCE 182 AA; 19765 MW; FF51475F9C0D82EC CRC64; MLQPLTEADG LILDIRYATP DNLAGRPIYS RPVALLLPEG RARLLAARDQ AAALGLRIKI FDAFRPIEAQ WALWHAVEDK RFVSDPRRGG VHPRGAAVDL TLCDAATGAE LPMGTGFDAV DPASAHGSLA VPVADQRNRA LLLGLMVAAG FEPYLLEWWH YQLPQPRRFP VLSASAVPDG PM //