ID F4HAH3_GALAU Unreviewed; 440 AA.
AC F4HAH3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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 OrderedLocusNames=UMN179_01328 {ECO:0000313|EMBL:AEC17347.1};
OS Gallibacterium anatis (strain UMN179) (Pasteurella anatis).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Gallibacterium.
OX NCBI_TaxID=1005058 {ECO:0000313|EMBL:AEC17347.1, ECO:0000313|Proteomes:UP000006908};
RN [1] {ECO:0000313|EMBL:AEC17347.1, ECO:0000313|Proteomes:UP000006908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN179 {ECO:0000313|EMBL:AEC17347.1,
RC ECO:0000313|Proteomes:UP000006908};
RX PubMed=21602325; DOI=10.1128/JB.05177-11;
RA Johnson T.J., Fernandez-Alarcon C., Bojesen A.M., Nolan L.K., Trampel D.W.,
RA Seemann T.;
RT "Complete genome sequence of Gallibacterium anatis strain UMN179, isolated
RT from a laying hen with peritonitis.";
RL J. Bacteriol. 193:3676-3677(2011).
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 ---------------------------------------------------------------------------
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; CP002667; AEC17347.1; -; Genomic_DNA.
DR RefSeq; WP_013746122.1; NC_015460.1.
DR AlphaFoldDB; F4HAH3; -.
DR STRING; 1005058.UMN179_01328; -.
DR MEROPS; M24.003; -.
DR KEGG; gan:UMN179_01328; -.
DR PATRIC; fig|1005058.3.peg.1317; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_050675_0_0_6; -.
DR Proteomes; UP000006908; Chromosome.
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 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 4..151
FT /note="Xaa-Pro dipeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21216"
FT DOMAIN 163..422
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT BINDING 240
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
FT BINDING 332
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
FT BINDING 377
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
FT BINDING 416
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
FT BINDING 416
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
SQ SEQUENCE 440 AA; 50540 MW; 1E199ED068FF360F CRC64;
METLFNAHLA RIQTIIQEAL SSCRLDGVWI YAGQADYYFV DDQTKSFHIN PYFNYVVPMP
QAEGSWLFLD GYSKPKLYFY QPKDYWYFVE ALPKAFWCEQ FEWQVFTQPQ QMQQEVNSRK
NCAFIGEDEA LAKSLGFYSI NDRKLLNILN YYRAYKSEYE IECIFRAQKP ALLGHQAAKQ
AFEQGKSEFD INAAYLQASQ QSDLNVPYGN IIALNEHGAV LHYNRLSHQA PETANSFLID
AGASYLGYAS DITRTYQQQT QPIFAELLRG MEQIKRDIIA DLCVGHNYLS YHTQLQQRIA
ELLAESELVK LPAQQIFDLG INRAFLPHGL GHLLGLQVHD IGGWQQNKRG AIKRPPEVYP
SLRCTRELAE GMVLTIEPGF YFIDLLLQPW RQSEYASKID WAMIDVLKAF GGIRTEDNIV
MRAEGAENLT VKMEQQLGLS
//
