ID A0A239RHP2_9BACT Unreviewed; 603 AA.
AC A0A239RHP2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (Putrescine degradation), contains GATase1-like domain {ECO:0000313|EMBL:SNU10420.1};
GN ORFNames=SAMN06298210_102182 {ECO:0000313|EMBL:SNU10420.1};
OS Prevotellaceae bacterium KH2P17.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae.
OX NCBI_TaxID=1945886 {ECO:0000313|EMBL:SNU10420.1, ECO:0000313|Proteomes:UP000214740};
RN [1] {ECO:0000313|EMBL:SNU10420.1, ECO:0000313|Proteomes:UP000214740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH2P17 {ECO:0000313|EMBL:SNU10420.1,
RC ECO:0000313|Proteomes:UP000214740};
RA Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FZRE01000002; SNU10420.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239RHP2; -.
DR Proteomes; UP000214740; 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:SNU10420.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000214740}.
FT ACT_SITE 126
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 232
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 234
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 603 AA; 66109 MW; 699C87B55FF30523 CRC64;
MNDFDLQSHL DSVYATFPEA SNRPVIGITS NYTNGDAALR DRYYTQVVAA GGTPVIIPPV
ADKDVIIGTL DRIDGLLLTG GGDYNPLWAG EEPLPQLHGI NSERDLPELL LTRLAFNRQI
PMLGICRGIQ TLALALGGTL MQDIAQGMPA AARLLKHSQD ADRQEPTHSV SIEPDSILHG
IYGAERLYVN SFHHQAVQDP GKRFRVTAQA PDGVTEAIES TEFKAVLGVQ WHPEWLQQEG
LKLFEWLVGE AGNFSVAKRL HHRVLTLDTH CDTPMFFPQG VNFAQRDPRI LVDLHKMADG
RQDAVTMVAY LPQPKPGEPF AEKIDIAGLQ KYNPQQAELL SHITPTAYAD FIFDKIEATV
HEHAASVAIA RTPAQLYENK RHGRKSVMLG IENGLALGSD LSNISHFAQR GVVYITLCHN
GDNQICDSAR GSGTHGGVSA FGEQVIREMN AQGIMVDLSH GAERSFYDAL DISQLPIVCS
HSNCRALCNV PRNLTDQQLR ALALKGGVAH TTLYAGFLRQ AGEADIRDAV AHLEHAISVM
GIEHVGLGTD FDGDGGIRGL ADSSELINFT ICLLRRKYSE QDIARIWGGN WLRVMTQVQN
ARK
//