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Database: UniProt
Entry: A0A255S9P2_9BACT
LinkDB: A0A255S9P2_9BACT
Original site: A0A255S9P2_9BACT 
ID   A0A255S9P2_9BACT        Unreviewed;       589 AA.
AC   A0A255S9P2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Fused gamma-glutamyl-gamma-aminobutyrate hydrolase/peptidase {ECO:0000313|EMBL:OYP49723.1};
GN   ORFNames=CIK97_06830 {ECO:0000313|EMBL:OYP49723.1};
OS   Prevotella sp. P3-120.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=2024220 {ECO:0000313|EMBL:OYP49723.1, ECO:0000313|Proteomes:UP000216094};
RN   [1] {ECO:0000313|EMBL:OYP49723.1, ECO:0000313|Proteomes:UP000216094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P3-120 {ECO:0000313|EMBL:OYP49723.1,
RC   ECO:0000313|Proteomes:UP000216094};
RA   Accetto T., Nograsek B., Avgustin G.;
RT   "Comparative genomics of non-oral Prevotella species.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:OYP49723.1}.
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DR   EMBL; NPJD01000044; OYP49723.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255S9P2; -.
DR   Proteomes; UP000216094; Unassembled WGS sequence.
DR   GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd01745; GATase1_2; 1.
DR   CDD; cd01301; rDP_like; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR008257; Pept_M19.
DR   InterPro; IPR011697; Peptidase_C26.
DR   PANTHER; PTHR10443:SF12; DIPEPTIDASE; 1.
DR   PANTHER; PTHR10443; MICROSOMAL DIPEPTIDASE; 1.
DR   Pfam; PF07722; Peptidase_C26; 1.
DR   Pfam; PF01244; Peptidase_M19; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1.
PE   4: Predicted;
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Hydrolase {ECO:0000313|EMBL:OYP49723.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216094}.
FT   ACT_SITE        126
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        233
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        235
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   589 AA;  65305 MW;  52810AD5241A2C9A CRC64;
     MNRFDWQAQL AKCHASFPAA THKPVIAITG NYGEGNCKLA QTYYKSVEDA GGVPIIMPPS
     AQTDTIINTL EHIDGLLISG GSDFNPLFAG EQPVVKLGGI NAERDLAELL TIRLAYDRQI
     PMLAICRGIQ ALAMALDGHV EQDISHRAQV KHSQDADRSE PTHSVKIEPD SILGSLYADT
     LKDNDGILYV NSFHHQAVDH CGPRFRTTAE SADGIIEAIE SREYKSIIGV QWHPECLVDG
     APLFQWLVKE SEHFYQACKL HERIITLDTH CDTPMFFPQG VDFGSRDKKI LVDLHKMTEG
     HQDATIMVAY LPQPKPGEDF PSIVDFDVKN PTEYADLIFD KIETMVAHNK SYLSIARTPA
     DLYANKKKGL KSIMLGIENG LAINGDLRKL RHFAERGIVY MTLCHNGDND ICDSARGCNT
     HGGVSDFGQQ VIRKMNKLGI MVDMSHAGER SFYDALDISQ QPIVCSHSSC RALCDHPRNL
     TDDQMRQLAA KGGVMQVTLY NGFLCKDGEA TVLDALAHLD HAINIMGIDH VGLGSDFDGD
     GGIRGLSCSS EMINFTRHLM AKRYSERDIQ KIWGRNFLRI MKQVQSAKS
//
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