ID Q6ME33_PARUW Unreviewed; 269 AA.
AC Q6ME33;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 07-JUN-2017, entry version 98.
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};
DE AltName: Full=PLP-independent amino acid racemase {ECO:0000256|HAMAP-Rule:MF_00197};
GN Name=dapF {ECO:0000256|HAMAP-Rule:MF_00197,
GN ECO:0000313|EMBL:CAF23166.1};
GN OrderedLocusNames=pc0442 {ECO:0000313|EMBL:CAF23166.1};
OS Protochlamydia amoebophila (strain UWE25).
OC Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC Candidatus Protochlamydia.
OX NCBI_TaxID=264201 {ECO:0000313|EMBL:CAF23166.1, ECO:0000313|Proteomes:UP000000529};
RN [1] {ECO:0000313|EMBL:CAF23166.1, ECO:0000313|Proteomes:UP000000529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWE25 {ECO:0000313|EMBL:CAF23166.1,
RC 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 -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00197,
CC ECO:0000256|SAAS:SAAS00734348}.
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, ECO:0000256|SAAS:SAAS00686236}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00197}.
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DR EMBL; BX908798; CAF23166.1; -; Genomic_DNA.
DR RefSeq; WP_011174992.1; NC_005861.1.
DR ProteinModelPortal; Q6ME33; -.
DR STRING; 264201.pc0442; -.
DR EnsemblBacteria; CAF23166; CAF23166; pc0442.
DR KEGG; pcu:pc0442; -.
DR eggNOG; ENOG4105E4Z; Bacteria.
DR eggNOG; COG0253; LUCA.
DR HOGENOM; HOG000220466; -.
DR KO; K01778; -.
DR OMA; MCGNGGR; -.
DR OrthoDB; POG091H01QC; -.
DR UniPathway; UPA00034; UER00025.
DR Proteomes; UP000000529; Chromosome.
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 Isomerase {ECO:0000256|HAMAP-Rule:MF_00197,
KW ECO:0000256|SAAS:SAAS00118214};
KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197,
KW ECO:0000256|SAAS:SAAS00028058};
KW Reference proteome {ECO:0000313|Proteomes:UP000000529}.
FT REGION 74 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 {ECO:0000256|PROSITE-ProRule:PRU10125}.
FT ACT_SITE 73 73 Proton donor. {ECO:0000256|HAMAP-Rule:
FT MF_00197}.
FT ACT_SITE 206 206 Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT MF_00197}.
FT BINDING 13 13 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 Could be important to modulate the pK
FT values of the two catalytic cysteine
FT residues. {ECO:0000256|HAMAP-Rule:
FT MF_00197}.
FT SITE 196 196 Could be important to modulate the pK
FT values of the two catalytic cysteine
FT residues. {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
//
