ID G9WP10_9FIRM Unreviewed; 295 AA.
AC G9WP10;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Proline iminopeptidase {ECO:0000256|ARBA:ARBA00021843, ECO:0000256|PIRNR:PIRNR005539};
DE Short=PIP {ECO:0000256|PIRNR:PIRNR005539};
DE EC=3.4.11.5 {ECO:0000256|ARBA:ARBA00012568, ECO:0000256|PIRNR:PIRNR005539};
DE AltName: Full=Prolyl aminopeptidase {ECO:0000256|ARBA:ARBA00029605, ECO:0000256|PIRNR:PIRNR005539};
GN ORFNames=HMPREF9625_01093 {ECO:0000313|EMBL:EHL10093.1};
OS Oribacterium parvum ACB1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Oribacterium.
OX NCBI_TaxID=796943 {ECO:0000313|EMBL:EHL10093.1, ECO:0000313|Proteomes:UP000018461};
RN [1] {ECO:0000313|Proteomes:UP000018461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACB1 {ECO:0000313|Proteomes:UP000018461};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cuomo C., Becnel J., Sanscrainte N., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACB1 {ECO:0000313|Proteomes:UP000018461};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Ward D., Feldgarden M., Gevers D., Sizova M., Hazen A.,
RA Epstein S., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M.,
RA Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J.,
RA McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Oribacterium sp. ACB1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Releases the N-terminal proline from various substrates.
CC {ECO:0000256|PIRNR:PIRNR005539}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001585,
CC ECO:0000256|PIRNR:PIRNR005539};
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088, ECO:0000256|PIRNR:PIRNR005539}.
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:EHL10093.1}.
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DR EMBL; AFZC01000018; EHL10093.1; -; Genomic_DNA.
DR RefSeq; WP_009534949.1; NZ_KE148312.1.
DR AlphaFoldDB; G9WP10; -.
DR STRING; 796943.HMPREF9625_01093; -.
DR MEROPS; S33.021; -.
DR GeneID; 84784973; -.
DR PATRIC; fig|796943.3.peg.1526; -.
DR HOGENOM; CLU_020336_15_0_9; -.
DR Proteomes; UP000018461; Unassembled WGS sequence.
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; PTHR43194; HYDROLASE ALPHA/BETA FOLD FAMILY; 1.
DR PANTHER; PTHR43194:SF5; PIMELOYL-[ACYL-CARRIER PROTEIN] METHYL ESTER ESTERASE; 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:0000256|PIRNR:PIRNR005539};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR005539};
KW Protease {ECO:0000256|PIRNR:PIRNR005539};
KW Reference proteome {ECO:0000313|Proteomes:UP000018461}.
FT DOMAIN 30..278
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005539-1"
FT ACT_SITE 246
FT /evidence="ECO:0000256|PIRSR:PIRSR005539-1"
FT ACT_SITE 273
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005539-1"
SQ SEQUENCE 295 AA; 33586 MW; 47AFEDB9C33B2EBD CRC64;
MAKITEGTMP YLGYETYYRI VGEKNPNKAP LLLLHGGPGS THNYFEVLDD LADRDNRQII
MYDQIGCGNS FVDGHPELWT KETWANELVA LREHLGLDKV HLLGQSWGGM LAIIYGCDYA
PKGVKSIVLS STLPYNAIWE SEQKRRVSYM TAEQQAAIKK AEDTGNYDDP DYLAAINVFM
EKYCYGVINE DSPECLTRKK KAGVEPYVVG WGPNEFTPTG TLKDYNYMEK LHSFAYPTLI
CDGAEDLCSP YIAKMMYDAI PNAKWELFAY SRHMCFVDEG PKYKEILLKW LNEND
//
