PEPD_HAEIN
ID PEPD_HAEIN Reviewed; 484 AA.
AC P44817;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cytosol non-specific dipeptidase;
DE EC=3.4.13.18;
DE AltName: Full=Aminoacyl-histidine dipeptidase;
DE AltName: Full=Beta-alanyl-histidine dipeptidase;
DE AltName: Full=Carnosinase;
DE AltName: Full=Peptidase D;
DE AltName: Full=Xaa-His dipeptidase;
DE Short=X-His dipeptidase;
GN Name=pepD; OrderedLocusNames=HI_0675;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Dipeptidase with broad substrate specificity. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of dipeptides, preferentially hydrophobic
CC dipeptides including prolyl amino acids.; EC=3.4.13.18;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. Can also use Co(2+).
CC {ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M20C family. {ECO:0000305}.
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DR EMBL; L42023; AAC22335.1; -; Genomic_DNA.
DR PIR; E64085; E64085.
DR RefSeq; NP_438835.1; NC_000907.1.
DR RefSeq; WP_005694602.1; NC_000907.1.
DR AlphaFoldDB; P44817; -.
DR SMR; P44817; -.
DR STRING; 71421.HI_0675; -.
DR MEROPS; M20.007; -.
DR DNASU; 950737; -.
DR EnsemblBacteria; AAC22335; AAC22335; HI_0675.
DR KEGG; hin:HI_0675; -.
DR PATRIC; fig|71421.8.peg.705; -.
DR eggNOG; COG2195; Bacteria.
DR HOGENOM; CLU_028526_0_0_6; -.
DR OMA; KGGYPGW; -.
DR PhylomeDB; P44817; -.
DR BioCyc; HINF71421:G1GJ1-710-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0103046; F:alanylglutamate dipeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070573; F:metallodipeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03890; M20_pepD; 1.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR001160; Peptidase_M20C.
DR PANTHER; PTHR43501; PTHR43501; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF016599; Xaa-His_dipept; 1.
DR PRINTS; PR00934; XHISDIPTASE.
DR TIGRFAMs; TIGR01893; aa-his-dipept; 1.
PE 3: Inferred from homology;
KW Cobalt; Dipeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..484
FT /note="Cytosol non-specific dipeptidase"
FT /id="PRO_0000185355"
FT ACT_SITE 78
FT /evidence="ECO:0000250"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 456
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 484 AA; 52888 MW; BA102E194DC96BA1 CRC64;
MSEITTLQPS LLWKWFDQIC AIPHPSHYED TLANFIVNWA KEKHFFVERD EVGNVLIRKP
ATKGMENHTP VVLQAHLDMV PQANEGNPHD FTKDPIQPYI DGEWVKARGT TLGSDNGIGL
ASTLAVLESN DLAHPPLEVL LTMTEETGMD GAKGLRHNWL QSEILINTDT EEIGEIYIGC
AGGINANFEI PVQYETNTFE HSAQITLKGL RGGHSGGDIH TGRANAIKVL ARVLAKLSQN
QPHFALSEIR GGSIRNAIPR EAAAVLAFNG DVKTIESAVE NLAVVLKEEL AIAEPNFTLF
VESAEKAPTV FTAQSTQTVI NALNVLPNGV IRNSDVVKNV VESSLSVGVL KTEGNVVKST
ILVRSLIESG KYYVTEMLSS LAILANAKVE FSAPYPGWQP VNDSTILDVT RKHYAEVLGE
QPVVKVIHAG LECGLLKEHY PNIEMISVGP TIRNAHSPDE KVEIATVQTY WDLLTRVLAD
IPAK
