ID Q8EHU8_SHEON Unreviewed; 486 AA.
AC Q8EHU8;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Aminoacyl-histidine/glycine-aspartate dipeptidase PepD {ECO:0000313|EMBL:AAN54185.1};
DE EC=3.4.13.18 {ECO:0000313|EMBL:AAN54185.1};
DE EC=3.4.13.20 {ECO:0000313|EMBL:AAN54185.1};
GN Name=pepD {ECO:0000313|EMBL:AAN54185.1};
GN OrderedLocusNames=SO_1115 {ECO:0000313|EMBL:AAN54185.1};
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN54185.1, ECO:0000313|Proteomes:UP000008186};
RN [1] {ECO:0000313|EMBL:AAN54185.1, ECO:0000313|Proteomes:UP000008186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1 {ECO:0000313|EMBL:AAN54185.1,
RC ECO:0000313|Proteomes:UP000008186};
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J.,
RA Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J.,
RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C.,
RA Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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DR EMBL; AE014299; AAN54185.1; -; Genomic_DNA.
DR RefSeq; NP_716740.1; NC_004347.2.
DR RefSeq; WP_011071358.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EHU8; -.
DR STRING; 211586.SO_1115; -.
DR MEROPS; M20.007; -.
DR PaxDb; 211586-SO_1115; -.
DR KEGG; son:SO_1115; -.
DR PATRIC; fig|211586.12.peg.1070; -.
DR eggNOG; COG2195; Bacteria.
DR HOGENOM; CLU_028526_0_0_6; -.
DR OrthoDB; 9773892at2; -.
DR PhylomeDB; Q8EHU8; -.
DR BioCyc; SONE211586:G1GMP-1027-MONOMER; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0103046; F:alanylglutamate dipeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0070573; F:metallodipeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd03890; M20_pepD; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR001160; Peptidase_M20C.
DR NCBIfam; TIGR01893; aa-his-dipept; 1.
DR PANTHER; PTHR43501; CYTOSOL NON-SPECIFIC DIPEPTIDASE; 1.
DR PANTHER; PTHR43501:SF1; CYTOSOL NON-SPECIFIC DIPEPTIDASE; 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 SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Dipeptidase {ECO:0000313|EMBL:AAN54185.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AAN54185.1};
KW Protease {ECO:0000313|EMBL:AAN54185.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008186}.
FT DOMAIN 208..291
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 486 AA; 52940 MW; 5B01598D4505B0CF CRC64;
MTALSQLYPQ PLWQWFEQIC AIPHPSKHEQ SLSQHIQAWA KQKQLDVVED AVGNVIIRKA
ATPGMEDRKV VVIQAHIDMV PQKNADKVHD FIKDPIEAYV DGDWVKAKGT TLGADNGIGM
ASALAILGSD DIKHGPLEVL LTIDEEAGMT GAFGLQAGML NAEILINTDS EQEGEIYMGC
AGGVDAQITL PMVWQASEQS YASFSLHLSG LKGGHSGVNI HLGRGNANKI LARFLFENAD
ELALELTQFT GGSLRNAIPR EANISFMLPA ENIDALKEKV HAFEALMRAE LAIADPDLRL
VLSNIATPKR VMSENSQNTL IDLLHVCPNG VMRMSDEVTG VTETSLNVGV ISTNDEEVGI
LCLIRSLIDS GRSQVEGMLN ALTNLAGADV EFSGAYPGWK PDNTSPVMAI VRETYESIYH
KEPVIMVIHA GLECGLFKKP YPEMDMVSIG PTIRYPHGPD EMVNITTVGQ YWDLLVAVLE
RIPVKA
//
