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Database: UniProt/TrEMBL
Entry: Q6ME33_PARUW
LinkDB: Q6ME33_PARUW
Original site: Q6ME33_PARUW 
ID   Q6ME33_PARUW            Unreviewed;       269 AA.
AC   Q6ME33;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   26-NOV-2014, entry version 75.
DE   RecName: Full=Diaminopimelate epimerase {ECO:0000256|HAMAP-Rule:MF_00197, ECO:0000256|SAAS:SAAS00028055};
DE            Short=DAP epimerase {ECO:0000256|HAMAP-Rule:MF_00197};
DE            EC=5.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00197, ECO:0000256|SAAS:SAAS00028063};
GN   Name=dapF {ECO:0000256|HAMAP-Rule:MF_00197};
GN   OrderedLocusNames=pc0442 {ECO:0000313|EMBL:CAF23166.1};
OS   Protochlamydia amoebophila (strain UWE25).
OC   Bacteria; Chlamydiae; Chlamydiales; Parachlamydiaceae;
OC   Candidatus Protochlamydia.
OX   NCBI_TaxID=264201 {ECO:0000313|EMBL:CAF23166.1, ECO:0000313|Proteomes:UP000000529};
RN   [1] {ECO:0000313|Proteomes:UP000000529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWE25 {ECO:0000313|Proteomes:UP000000529};
RX   PubMed=15073324; DOI=10.1126/science.1096330;
RA   Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA   Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D.,
RA   Rattei T., Mewes H.-W., Wagner M.;
RT   "Illuminating the evolutionary history of chlamydiae.";
RL   Science 304:728-730(2004).
CC   -!- FUNCTION: Catalyzes the stereoinversion of LL-2,6-
CC       diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-
CC       DAP), a precursor of L-lysine and an essential component of the
CC       bacterial peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- CATALYTIC ACTIVITY: LL-2,6-diaminoheptanedioate = meso-
CC       diaminoheptanedioate. {ECO:0000256|HAMAP-Rule:MF_00197,
CC       ECO:0000256|SAAS:SAAS00028060}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step
CC       1/1. {ECO:0000256|HAMAP-Rule:MF_00197,
CC       ECO:0000256|SAAS:SAAS00028059}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197,
CC       ECO:0000256|SAAS:SAAS00028061}.
CC   -!- SIMILARITY: Belongs to the diaminopimelate epimerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00197}.
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DR   EMBL; BX908798; CAF23166.1; -; Genomic_DNA.
DR   RefSeq; YP_007441.1; NC_005861.1.
DR   ProteinModelPortal; Q6ME33; -.
DR   STRING; 264201.pc0442; -.
DR   PRIDE; Q6ME33; -.
DR   EnsemblBacteria; CAF23166; CAF23166; pc0442.
DR   GeneID; 2780463; -.
DR   KEGG; pcu:pc0442; -.
DR   PATRIC; 31996186; VBICanPro72727_0446.
DR   eggNOG; COG0253; -.
DR   HOGENOM; HOG000220466; -.
DR   KO; K01778; -.
DR   OMA; LIVEPPY; -.
DR   OrthoDB; EOG6ND0M5; -.
DR   BioCyc; PAMO264201:GH0M-453-MONOMER; -.
DR   UniPathway; UPA00034; UER00025.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00197; DAP_epimerase; 1.
DR   InterPro; IPR018510; DAP_epimerase_AS.
DR   InterPro; IPR001653; DAP_epimerase_DapF.
DR   PANTHER; PTHR31689; PTHR31689; 1.
DR   Pfam; PF01678; DAP_epimerase; 2.
DR   TIGRFAMs; TIGR00652; DapF; 1.
DR   PROSITE; PS01326; DAP_EPIMERASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197,
KW   ECO:0000256|SAAS:SAAS00028064};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000529};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197,
KW   ECO:0000256|SAAS:SAAS00028054};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00197,
KW   ECO:0000256|SAAS:SAAS00028056};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00197,
KW   ECO:0000256|SAAS:SAAS00028057};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197,
KW   ECO:0000256|SAAS:SAAS00028058};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000529}.
FT   REGION       73     75       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00197}.
FT   REGION      196    197       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00197}.
FT   REGION      207    208       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00197}.
FT   ACT_SITE     73     73       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00197}.
FT   ACT_SITE    206    206       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00197}.
FT   BINDING      13     13       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   BINDING      46     46       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   BINDING      64     64       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   BINDING     178    178       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   SITE        146    146       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00197}.
FT   SITE        196    196       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00197}.
FT   DISULFID     73    206       Size: 249-333. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
SQ   SEQUENCE   269 AA;  30111 MW;  860051C3331CA36A CRC64;
     MQWSFTKYVG CGNDFILFDN RNGKFPFSIP LIQQLCHRQW GVGADGIILL ENSTIAHARM
     RIFNADGSEA EMCGNGLRCL IDWMESLNIL HSIYSIETNN HVLKAWKSAS NITIEMGSPN
     KLNWNVPISF ESKIYYVHSL NTGVPHIILF AENIEQFPLE RMGPFIRYHP LWKPDGTNFS
     IVQHLHGQTF MIRTYERGVE AETLACGTGA TAAALAAAFQ YRLSAPISMQ TRSGICLEIG
     FTLLNQKFTN VTMTGPALAV FNGSIKLES
//
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