ID D5ESM6_PRER2 Unreviewed; 290 AA.
AC D5ESM6;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Prolyl aminopeptidase {ECO:0000313|EMBL:ADE82599.1};
DE EC=3.4.11.5 {ECO:0000313|EMBL:ADE82599.1};
GN Name=pip {ECO:0000313|EMBL:ADE82599.1};
GN OrderedLocusNames=PRU_1316 {ECO:0000313|EMBL:ADE82599.1};
OS Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Xylanibacter.
OX NCBI_TaxID=264731 {ECO:0000313|EMBL:ADE82599.1, ECO:0000313|Proteomes:UP000000927};
RN [1] {ECO:0000313|EMBL:ADE82599.1, ECO:0000313|Proteomes:UP000000927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000313|Proteomes:UP000000927};
RX PubMed=20585943; DOI=10.1007/s00248-010-9692-8;
RG North American Consortium for Rumen Bacteria;
RA Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I.,
RA Coutinho P.M., Henrissat B., Nelson K.E.;
RT "Comparative genome analysis of Prevotella ruminicola and Prevotella
RT bryantii: insights into their environmental niche.";
RL Microb. Ecol. 60:721-729(2010).
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088, ECO:0000256|PIRNR:PIRNR005539}.
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DR EMBL; CP002006; ADE82599.1; -; Genomic_DNA.
DR RefSeq; WP_013064585.1; NC_014033.1.
DR AlphaFoldDB; D5ESM6; -.
DR STRING; 264731.PRU_1316; -.
DR ESTHER; prer2-d5esm6; Proline_iminopeptidase.
DR MEROPS; S33.021; -.
DR KEGG; pru:PRU_1316; -.
DR eggNOG; COG2267; Bacteria.
DR HOGENOM; CLU_020336_15_1_10; -.
DR Proteomes; UP000000927; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR002410; Peptidase_S33.
DR InterPro; IPR005945; Pro_imino_pep.
DR NCBIfam; TIGR01250; pro_imino_pep_2; 1.
DR PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR PANTHER; PTHR43798:SF5; MONOACYLGLYCEROL LIPASE ABHD6; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF005539; Pept_S33_TRI_F1; 1.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:ADE82599.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR005539, ECO:0000313|EMBL:ADE82599.1};
KW Protease {ECO:0000313|EMBL:ADE82599.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000927}.
FT DOMAIN 27..273
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 102
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005539-1"
FT ACT_SITE 241
FT /evidence="ECO:0000256|PIRSR:PIRSR005539-1"
FT ACT_SITE 268
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005539-1"
SQ SEQUENCE 290 AA; 33228 MW; D6B807AC35ADDCAD CRC64;
MITEGYMPFM GYQTYYRIVG EASEKTPLLL LHGGPGSTHN YFEVLDCIAE TGRQVISYDQ
IGCGNSYLDG HPELWTQKTW IDELIAIREY LQLDAVHILG QSWGAMQAIA YVIDHQPQGI
KSLILSSGHA SSSLWASEQH RLIKYLSDED QEAIRHAEAT GKWDDEAYLQ ANNHYFEQFV
ISVDEHSPEC LRRPKRAGAE AYLYGWGPNE YQPLGSLKDF EYTDKLDQIS QPTLICSGTR
DICTPVVAAS LYEHIPHSQW HLFRHSRHTC FIDAHQEYCQ VLTKWLEEND
//
