ID   A0A0Q3WHT7_BRECH        Unreviewed;       480 AA.
AC   A0A0Q3WHT7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Xaa-His dipeptidase {ECO:0000313|EMBL:KQL44980.1};
GN   ORFNames=AN963_26995 {ECO:0000313|EMBL:KQL44980.1};
OS   Brevibacillus choshinensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=54911 {ECO:0000313|EMBL:KQL44980.1, ECO:0000313|Proteomes:UP000051063};
RN   [1] {ECO:0000313|EMBL:KQL44980.1, ECO:0000313|Proteomes:UP000051063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8552 {ECO:0000313|EMBL:KQL44980.1,
RC   ECO:0000313|Proteomes:UP000051063};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQL44980.1}.
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DR   EMBL; LJJB01000013; KQL44980.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q3WHT7; -.
DR   STRING; 54911.AN963_26995; -.
DR   PATRIC; fig|54911.3.peg.3483; -.
DR   Proteomes; UP000051063; Unassembled WGS sequence.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.30.70.360; -; 2.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR010964; M20A_pepV-rel.
DR   InterPro; IPR002933; Peptidase_M20.
DR   NCBIfam; TIGR01887; dipeptidaselike; 1.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF33; DIPEPTIDASE SAOUHSC_01868-RELATED; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   4: Predicted;
KW   Dipeptidase {ECO:0000256|ARBA:ARBA00022997};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022997};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   480 AA;  52348 MW;  D7A8A56D4FE92DDC CRC64;
     MINWYEEVNR RKEDLLQDLD GLLRIPSVKN LETSGPGAPM GKEIGRALGY MLDLSAQHGF
     RTANLDGYVG YAELGGSAED GYIAVLGHLD VVAATGNWTS PPYEPTIRDG KLHARGAIDD
     KGPTLAAYYG LKIVKELGLP LKHNVRFIFG TDEESGSRCM ARYRQTEKLP IAGFTPDADY
     PIVHAEKGQI NTRVMLERSV EHAPVGLEGK WYLHSFFGGG TANMVPESAR AIIAGEAGSL
     GELAAEYTAY CESRGRRGIS RIEAGQIILE MEGKAAHGME PQLGVNAALE LIHFLAPLSF
     QPDAERFLHC VETYLFEDYA GVALGIANED EISGALTINS GILQFEPEGE SFFYINLRYP
     VTDEASRILD TITKQVGKYG FAMEPPLLKK GHHVAKDHPM IGILQQIYQD TTGLVPTLLS
     TGGGTYAYHI GNGVAFGPLF PGKTSLAHQA DEYIEVEDLL LSAAMYARAI YELANADYDK
//