ID A0A0X8HED7_9GAMM Unreviewed; 435 AA.
AC A0A0X8HED7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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_1 {ECO:0000313|EMBL:AMD00965.1};
GN Synonyms=pepQ {ECO:0000256|HAMAP-Rule:MF_01279};
GN ORFNames=LOKO_01897 {ECO:0000313|EMBL:AMD00965.1};
OS Halomonas chromatireducens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=507626 {ECO:0000313|EMBL:AMD00965.1, ECO:0000313|Proteomes:UP000063387};
RN [1] {ECO:0000313|EMBL:AMD00965.1, ECO:0000313|Proteomes:UP000063387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMD00965.1,
RC ECO:0000313|Proteomes:UP000063387};
RX PubMed=26988058;
RA Sharko F.S., Shapovalova A.A., Tsygankova S.V., Komova A.V.,
RA Boulygina E.S., Teslyuk A.B., Gotovtsev P.M., Namsaraev Z.B.,
RA Khijniak T.V., Nedoluzhko A.V., Vasilov R.G.;
RT "Draft Genome Sequence of 'Halomonas chromatireducens' Strain AGD 8-3, a
RT Haloalkaliphilic Chromate- and Selenite-Reducing Gammaproteobacterium.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|EMBL:AMD00965.1, ECO:0000313|Proteomes:UP000063387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMD00965.1,
RC ECO:0000313|Proteomes:UP000063387};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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}.
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DR EMBL; CP014226; AMD00965.1; -; Genomic_DNA.
DR RefSeq; WP_066448105.1; NZ_CP014226.1.
DR AlphaFoldDB; A0A0X8HED7; -.
DR STRING; 507626.LOKO_01897; -.
DR KEGG; hco:LOKO_01897; -.
DR PATRIC; fig|507626.3.peg.1893; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000063387; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000063387}.
FT DOMAIN 10..150
FT /note="Xaa-Pro dipeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21216"
FT DOMAIN 164..423
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT BINDING 241
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
FT BINDING 252
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
FT BINDING 252
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
FT BINDING 334
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
FT BINDING 378
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
FT BINDING 417
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
FT BINDING 417
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
SQ SEQUENCE 435 AA; 47749 MW; 7FFFCCB4D5C8B302 CRC64;
MTDPLAELQR GHLDWLEQRY AETLSRLGYD GVLIFSGQPA LHFGDDQHAS FQAYGHFQHW
TGQAYLTHSW LLVCPGNLPV LYLHSPDDFW HLPASLPQEA WTERVEVVKG RFDVPPALPR
GRYAVIGDVD VATAGALGAD PNPEALLMAL DEGRVRKSEY EVACIGRANR QAMAGHIAAR
DAFLSGAAEL DVQLAYLQAS RQRESQVPYG NIVGINAHGG VLHYQHYDTL PPKKQRSLLV
DAGHRYHGYC ADITRTWAGG QADEVFPPLI KGVAHIQQQL IAAIRPGVDY AVLHEQMHEL
LAALLVEHRI VLGSPESAVA NGITRAFCPH GLGHLLGIQV HDVAGRRAAN GMALPPPDEH
PALRLTRELE AGMVVTIEPG LYVIPMLLDP LRQGPVGREV NWERVERLAP HGGIRIEDNV
LVTSDTAKNL TPEAE
//
