ID A0A0E0NBX8_ORYRU Unreviewed; 506 AA.
AC A0A0E0NBX8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Xaa-Pro dipeptidase {ECO:0000256|ARBA:ARBA00044141};
DE EC=3.4.13.9 {ECO:0000256|ARBA:ARBA00044051};
DE AltName: Full=Imidodipeptidase {ECO:0000256|ARBA:ARBA00044351};
DE AltName: Full=Peptidase D {ECO:0000256|ARBA:ARBA00044252};
DE AltName: Full=Proline dipeptidase {ECO:0000256|ARBA:ARBA00044284};
OS Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI02G09260.5, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI02G09260.5}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + Xaa-L-Pro dipeptide = an L-alpha-amino acid + L-proline;
CC Xref=Rhea:RHEA:76407, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869,
CC ChEBI:CHEBI:60039, ChEBI:CHEBI:195196; EC=3.4.13.9;
CC Evidence={ECO:0000256|ARBA:ARBA00043793};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. Eukaryotic-type
CC prolidase subfamily. {ECO:0000256|ARBA:ARBA00043990}.
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DR AlphaFoldDB; A0A0E0NBX8; -.
DR SMR; A0A0E0NBX8; -.
DR EnsemblPlants; ORUFI02G09260.5; ORUFI02G09260.5; ORUFI02G09260.
DR Gramene; ORUFI02G09260.5; ORUFI02G09260.5; ORUFI02G09260.
DR HOGENOM; CLU_017266_1_2_1; -.
DR OMA; YVTDCDL; -.
DR Proteomes; UP000008022; Unassembled WGS sequence.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR CDD; cd01087; Prolidase; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR InterPro; IPR007865; Aminopep_P_N.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR PANTHER; PTHR48392; -; 1.
DR PANTHER; PTHR48392:SF2; PEPTIDASE D; 1.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008022}.
FT DOMAIN 20..164
FT /note="Aminopeptidase P N-terminal"
FT /evidence="ECO:0000259|SMART:SM01011"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 506 AA; 56308 MW; 5879DB75C8168DFC CRC64;
MAAAAAAAPP SSSSLAPPEV PMELHAGNRD RLVAALRAHL SASGRPLRGL VLLQGGEEQT
RYCTDHLELF RQESYFAYLF GVREPGFYGA IDIVSGQSIL FSPRLPADYA VWMGEIKPLS
YFKDRYKVDM VFYVDEITQV LQDRFSDHGK PLLFVLYGKN TDSGNYSKPA SFEGMEKFDS
DLSTLHPILT ECRVIKSDME LALIQYANDV SSEAHIEVMR RAKPGMKEYQ LESIFLHHVY
MYGGCRHCSY TCICATGENS SVLHYGHAAA PNDRTLNDGD MALMDMGGEY HCYGSDITCS
YPINGKFNSN QTIVYNAVLK AHNAVIAHMR PGVNWLDMHK LAEQTILESL KNERILHGDV
TDMMAQRLGA VFMPHGLGHL LGIDTHDPGG YPEGLERPKE PGLSSLRTIR ELKEGMVITV
EPGCYFIDAL LIPARDDPVS SKFFNWEEIE KYKSFGGVRI ESDVYVTAHG CKNLTNCPRE
TWEIEAVMAG APWPVRATNN SLSKAS
//
