ID A0A093JBT8_FULGA Unreviewed; 479 AA.
AC A0A093JBT8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Cytosolic non-specific dipeptidase {ECO:0000256|ARBA:ARBA00041164};
DE EC=3.4.13.18 {ECO:0000256|ARBA:ARBA00038976};
DE AltName: Full=CNDP dipeptidase 2 {ECO:0000256|ARBA:ARBA00042010};
DE AltName: Full=Threonyl dipeptidase {ECO:0000256|ARBA:ARBA00041744};
DE Flags: Fragment;
GN ORFNames=N327_01785 {ECO:0000313|EMBL:KFW11428.1};
OS Fulmarus glacialis (Northern fulmar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Procellariiformes; Procellariidae;
OC Fulmarus.
OX NCBI_TaxID=30455 {ECO:0000313|EMBL:KFW11428.1, ECO:0000313|Proteomes:UP000053806};
RN [1] {ECO:0000313|EMBL:KFW11428.1, ECO:0000313|Proteomes:UP000053806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N327 {ECO:0000313|EMBL:KFW11428.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactate + L-phenylalanine = H2O + N-[(S)-lactoyl]-L-
CC phenylalanine; Xref=Rhea:RHEA:66724, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16651, ChEBI:CHEBI:58095, ChEBI:CHEBI:167456;
CC Evidence={ECO:0000256|ARBA:ARBA00036214};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66725;
CC Evidence={ECO:0000256|ARBA:ARBA00036214};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:66726;
CC Evidence={ECO:0000256|ARBA:ARBA00036214};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-cysteinylglycine = glycine + L-cysteine;
CC Xref=Rhea:RHEA:28783, ChEBI:CHEBI:15377, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:61694;
CC Evidence={ECO:0000256|ARBA:ARBA00023673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28784;
CC Evidence={ECO:0000256|ARBA:ARBA00023673};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-seryl-L-threonine = L-serine + L-threonine;
CC Xref=Rhea:RHEA:67372, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57926, ChEBI:CHEBI:169955;
CC Evidence={ECO:0000256|ARBA:ARBA00036410};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67373;
CC Evidence={ECO:0000256|ARBA:ARBA00036410};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-threonyl-L-serine = L-serine + L-threonine;
CC Xref=Rhea:RHEA:67364, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57926, ChEBI:CHEBI:169954;
CC Evidence={ECO:0000256|ARBA:ARBA00036500};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67365;
CC Evidence={ECO:0000256|ARBA:ARBA00036500};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-threonyl-L-threonine = 2 L-threonine;
CC Xref=Rhea:RHEA:67360, ChEBI:CHEBI:15377, ChEBI:CHEBI:57926,
CC ChEBI:CHEBI:169953; Evidence={ECO:0000256|ARBA:ARBA00036626};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67361;
CC Evidence={ECO:0000256|ARBA:ARBA00036626};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of dipeptides, preferentially hydrophobic
CC dipeptides including prolyl amino acids.; EC=3.4.13.18;
CC Evidence={ECO:0000256|ARBA:ARBA00036421};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR037242-3};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR037242-3};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; KK609796; KFW11428.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093JBT8; -.
DR MEROPS; M20.005; -.
DR Proteomes; UP000053806; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR CDD; cd05676; M20_dipept_like_CNDP; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR017153; CNDP/DUG1.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR PANTHER; PTHR43270:SF11; CYTOSOLIC NON-SPECIFIC DIPEPTIDASE; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037242; CNDP_dipeptidase; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|PIRSR:PIRSR037242-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037242-3};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022645};
KW Reference proteome {ECO:0000313|Proteomes:UP000053806}.
FT DOMAIN 212..370
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 105
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-1"
FT ACT_SITE 170
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-1"
FT BINDING 103
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 136
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 136
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 171
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 199
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 199
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 232
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 334
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 347
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 421
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 449
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 449
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT SITE 232
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW11428.1"
FT NON_TER 479
FT /evidence="ECO:0000313|EMBL:KFW11428.1"
SQ SEQUENCE 479 AA; 53524 MW; 5DA9E9B092476543 CRC64;
SGQKMSALET LFKYIDEHQD LYIQRLAQWV AIQSVSAWPE KRAEIRCMME VAAKDIERLG
GTTQLMDIGK QKLPDGSEIP LPPIVLGTLG SDPCKKTVCV YGHLDVQPAA LEDGWDSEPF
TLVEREGKLY GRGSTDDKGP VLAWLNALEA YQQTNQAFPV NVKFCLEGME ESGSEGLDEL
IFAQRDTFFK DVDYVCISDN YWLGKKKPCI TYGLRGICYY FIEVECSDKD LHSGVYGGSV
HEAMTDLITL MGSLIDKKGK ILIPGLNEAV APVTDEELAL YEKIDFDLEE YAKDVGATKL
LHDTKRDILM HRWRYPSLSL HGIEGAFSAS GAKTVIPRKV IGKFSIRLVP NMTPEEVTKH
VEDYVSKKFA ELQSPNKFRV YLGHGGKPWV SDFNHPHYMA GRRAMKTVFG VEPDLTREGG
SIPVTLTFQE ATGKNVMLLP VGAADDGAHS QNEKLNRYNY IQGVKMLGAY LYEVSQLKD
//
