(data stored in SCRATCH zone)

SWISSPROT: A0KFK8_AERHH

ID   A0KFK8_AERHH            Unreviewed;       534 AA.
AC   A0KFK8;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   13-FEB-2019, entry version 65.
DE   RecName: Full=Dipeptidase {ECO:0000256|RuleBase:RU364089};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU364089};
GN   OrderedLocusNames=AHA_0501 {ECO:0000313|EMBL:ABK39780.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK39780.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK39780.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino
CC         acid; Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:59869, ChEBI:CHEBI:77460;
CC         Evidence={ECO:0000256|RuleBase:RU364089};
CC   -!- SIMILARITY: Belongs to the peptidase C69 family.
CC       {ECO:0000256|RuleBase:RU364089}.
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DR   EMBL; CP000462; ABK39780.1; -; Genomic_DNA.
DR   RefSeq; WP_011704474.1; NC_008570.1.
DR   RefSeq; YP_855034.1; NC_008570.1.
DR   STRING; 380703.AHA_0501; -.
DR   MEROPS; C69.001; -.
DR   EnsemblBacteria; ABK39780; ABK39780; AHA_0501.
DR   GeneID; 4490083; -.
DR   KEGG; aha:AHA_0501; -.
DR   PATRIC; fig|380703.7.peg.494; -.
DR   eggNOG; ENOG4105DZW; Bacteria.
DR   eggNOG; COG4690; LUCA.
DR   HOGENOM; HOG000271092; -.
DR   OMA; NTPRTWY; -.
DR   BioCyc; AHYD380703:G1G7B-502-MONOMER; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR005322; Peptidase_C69.
DR   PANTHER; PTHR12994; PTHR12994; 1.
DR   Pfam; PF03577; Peptidase_C69; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KFK8.
DR   SWISS-2DPAGE; A0KFK8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Dipeptidase {ECO:0000256|RuleBase:RU364089};
KW   Hydrolase {ECO:0000256|RuleBase:RU364089};
KW   Protease {ECO:0000256|RuleBase:RU364089};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756}.
SQ   SEQUENCE   534 AA;  59190 MW;  288D04EC937F6B4F CRC64;
     MDEMFASSTM SSTIPRQRIG GRSLCGRPAS HRLAFTHSYA SGNPMKKHTL SLLSATLLTL
     LGTSADACTG LIVGKGASAD GSVMIARNED FGVNNWNKYL AFRSAQQNEG KVWKLGNGLE
     VPMPKAFFAY SAIRDWDATS SDPAGKYYEE RGINEFNVAI SATTSAEVND KAQKADPLIE
     KGVIEAIIPT LILPQAKTAK EGVALLGRYV EQYGAGEGNS LYLADVNEAW LMEIGSGHHW
     IAVRVPDDSY AMVANGLRIH GVNLDSADVL HSPKLLEFVR EHKLLDNADP KEFNFAKAFG
     VIADPYNVDR EWLGQKMLTA SHPQPTRQAQ YPLFMKPDAP IAVPDVARLL SATYEGTPLA
     GKAERPIRID RQLESHVIQL RKEMPKELQG LIWQSYGVLA ESVMVPLYNT LESYPLPYRT
     GSDSYSDDSA YWQFRSLTAL ASADPDKYLP LLRGVWSKES SKLYQEVALL DQSLKQAYAS
     DKATAIGLAA DYSYGQLEQT YQMAKELRYK LMTDLTKRTE QKYSPEEFKK IMSL
//

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