ID A0A1H8YTH4_9FIRM Unreviewed; 602 AA.
AC A0A1H8YTH4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 ORFNames=SAMN02910382_00205 {ECO:0000313|EMBL:SEP55331.1};
OS Butyrivibrio sp. TB.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1520809 {ECO:0000313|EMBL:SEP55331.1, ECO:0000313|Proteomes:UP000198682};
RN [1] {ECO:0000313|EMBL:SEP55331.1, ECO:0000313|Proteomes:UP000198682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TB {ECO:0000313|EMBL:SEP55331.1,
RC ECO:0000313|Proteomes:UP000198682};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOER01000001; SEP55331.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8YTH4; -.
DR Proteomes; UP000198682; Unassembled WGS sequence.
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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd14817; D-Ala-D-Ala_dipeptidase_VanX; 1.
DR Gene3D; 3.30.1380.10; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR HAMAP; MF_01924; A_A_dipeptidase; 1.
DR InterPro; IPR000755; A_A_dipeptidase.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR PANTHER; PTHR43126; D-ALANYL-D-ALANINE DIPEPTIDASE; 1.
DR PANTHER; PTHR43126:SF1; D-ALANYL-D-ALANINE DIPEPTIDASE; 1.
DR Pfam; PF12710; HAD; 1.
DR Pfam; PF01427; Peptidase_M15; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Dipeptidase {ECO:0000256|HAMAP-Rule:MF_01924};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01924};
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 233
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
FT SITE 123
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
SQ SEQUENCE 602 AA; 68306 MW; 6FAD4A508F05C5A5 CRC64;
MKFLKKLQTC TIVVVMLTVT IFCSSGKLSS VYDSFNLIGN NVYASGDYKY SVDSSDFVLL
TDVIPDAILE IRYYSTYNFV GDRITGYEEP IALLTKEAAA ALKQASDEFN SLGYRLKIYD
AYRPQMAVTH FANWALDVND TRMKAFFYPE LDKSVLFEQG YIDAHSGHSR GSTLDLTLFD
MNTEKEVDMG GTFDYFGELS HPDYTGITEQ QYANRMLLQS VMVKHGFKPL PEEWWHFTLV
DEPYPDTYFD FPVSRSSLLT NASDIEDQNN NNVKEQSDEG VLDPLSYWTT ESAARTSLVS
YVASVTDENS PDFIPVRDRI AVFDLDGTLF CETDPNYFDY CLLEYRVLDD PTYKDKASDF
EKEVALKIRD QNQNHTSYKG LEVDHGKAVA SAFAGMTIEE FNQYIQAFKA QPMPGYNNMT
RGQSFYLPMV QVVNFLQAYD FTVYIVSGTD RFIVRGIIDN SILDIPPRQI IGSDETIKSN
DQGDEDGLNY VFEDDDVLIL GGEFIVKNLK MNKVSVIAQE IGQQPVLSFG NSTGDLSMCE
YVVSNNKYKS MAFMLCCDDT VRENGNVEKA DKMYALCDEC DFVPISMKND WTTIYGDNVT
RK
//
