ID A0A7X1BUA1_9ENTR Unreviewed; 443 AA. AC A0A7X1BUA1; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 29-MAY-2024, entry version 12. DE RecName: Full=Xaa-Pro dipeptidase {ECO:0000256|HAMAP-Rule:MF_01279}; DE Short=X-Pro dipeptidase {ECO:0000256|HAMAP-Rule:MF_01279}; DE EC=3.4.13.9 {ECO:0000256|HAMAP-Rule:MF_01279}; DE AltName: Full=Imidodipeptidase {ECO:0000256|HAMAP-Rule:MF_01279}; DE AltName: Full=Proline dipeptidase {ECO:0000256|HAMAP-Rule:MF_01279}; DE Short=Prolidase {ECO:0000256|HAMAP-Rule:MF_01279}; GN Name=pepQ {ECO:0000256|HAMAP-Rule:MF_01279, GN ECO:0000313|EMBL:MBC2622792.1}; GN ORFNames=H7I73_24450 {ECO:0000313|EMBL:MBC2622792.1}; OS Citrobacter cronae. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=1748967 {ECO:0000313|EMBL:MBC2622792.1, ECO:0000313|Proteomes:UP000548504}; RN [1] {ECO:0000313|EMBL:MBC2622792.1, ECO:0000313|Proteomes:UP000548504} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FF141 {ECO:0000313|EMBL:MBC2622792.1, RC ECO:0000313|Proteomes:UP000548504}; RA Zheng B.; RT "Emergence and comparative genomics analysis of Citrobacter in Fennec fox RT imported from North Africa to China."; RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Splits dipeptides with a prolyl residue in the C-terminal CC position. {ECO:0000256|HAMAP-Rule:MF_01279}. 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|HAMAP-Rule:MF_01279}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01279}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01279}; CC -!- SIMILARITY: Belongs to the peptidase M24B family. Bacterial-type CC prolidase subfamily. {ECO:0000256|HAMAP-Rule:MF_01279}. 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:MBC2622792.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JACLAG010000011; MBC2622792.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7X1BUA1; -. DR Proteomes; UP000548504; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004177; F:aminopeptidase activity; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016795; F:phosphoric triester hydrolase activity; IEA:InterPro. DR GO; GO:0102009; F:proline dipeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 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 HAMAP; MF_01279; X_Pro_dipeptid; 1. DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD. DR InterPro; IPR036005; Creatinase/aminopeptidase-like. DR InterPro; IPR048819; PepQ_N. DR InterPro; IPR000994; Pept_M24. DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS. DR InterPro; IPR022846; X_Pro_dipept. DR PANTHER; PTHR43226; XAA-PRO AMINOPEPTIDASE 3; 1. DR PANTHER; PTHR43226:SF4; XAA-PRO AMINOPEPTIDASE 3; 1. DR Pfam; PF21216; PepQ_N; 1. DR Pfam; PF00557; Peptidase_M24; 1. DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1. DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1. PE 3: Inferred from homology; KW Dipeptidase {ECO:0000256|ARBA:ARBA00022997, ECO:0000256|HAMAP- KW Rule:MF_01279}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01279}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01279}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01279}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP- KW Rule:MF_01279}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01279}. FT DOMAIN 7..157 FT /note="Xaa-Pro dipeptidase N-terminal" FT /evidence="ECO:0000259|Pfam:PF21216" FT DOMAIN 168..430 FT /note="Peptidase M24" FT /evidence="ECO:0000259|Pfam:PF00557" FT BINDING 246 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279" FT BINDING 257 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279" FT BINDING 257 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279" FT BINDING 339 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279" FT BINDING 384 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279" FT BINDING 423 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279" FT BINDING 423 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279" SQ SEQUENCE 443 AA; 50165 MW; 51D76B64049F6D8A CRC64; MESLAALYKN HIVTLKERAR DALERFKLDA LLIHSGELVN VFLDDHPYPF KVNPQFKAWV PVTQVPNCWL LVDGVNKPKL WFYLPVDYWH NVEPLPTSFW TEEIEIIALP KADGIGSQLP AARGNIGYIG PVPERALQLD IAASNINPKG VIDYLHYYRA FKTDYELACM REAQKMAVNG HRAAEEAFRS GMSEFDINLA YLTATGHRDT DVPYSNIVAL NEHASVLHYT KLDHQAPSEI RSFLLDAGAE YNGYAADLTR TWSAKSDNDY AHLVKDVNDE ELALIATMKA GTSYVDYHIQ FHQRIAKLLR KHQIITDMSE EAMVENDLTG PFMPHGIGHP LGLQVHDVAG FMQDDSGTHL AAPSKYPYLR CTRVLQPGMV LTIEPGIYFI ESLLAPWREG QFSKHFNWQK IEALKPFGGI RIEDNVVVHE NNIENMTRDL KLA //