(data stored in SCRATCH zone)

SWISSPROT: Q5LX66_RUEPO

ID   Q5LX66_RUEPO            Unreviewed;       269 AA.
AC   Q5LX66;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, 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:AAV93597.1};
GN   OrderedLocusNames=SPO0278 {ECO:0000313|EMBL:AAV93597.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93597.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93597.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93597.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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:
CC       Reaction=LL-2,6-diaminoheptanedioate = meso-2,6-diaminopimelate;
CC         Xref=Rhea:RHEA:15393, ChEBI:CHEBI:57609, ChEBI:CHEBI:57791;
CC         EC=5.1.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00197,
CC         ECO:0000256|SAAS:SAAS01119439};
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; CP000031; AAV93597.1; -; Genomic_DNA.
DR   STRING; 246200.SPO0278; -.
DR   EnsemblBacteria; AAV93597; AAV93597; SPO0278.
DR   KEGG; sil:SPO0278; -.
DR   eggNOG; ENOG4105E4Z; Bacteria.
DR   eggNOG; COG0253; LUCA.
DR   HOGENOM; HOG000220466; -.
DR   KO; K01778; -.
DR   OMA; MCGNGGR; -.
DR   UniPathway; UPA00034; UER00025.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
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;
DR   PRODOM; Q5LX66.
DR   SWISS-2DPAGE; Q5LX66.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197,
KW   ECO:0000256|SAAS:SAAS00028064};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
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, ECO:0000313|EMBL:AAV93597.1};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197,
KW   ECO:0000256|SAAS:SAAS00028058};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023}.
FT   REGION       71     72       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00197}.
FT   REGION      198    199       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00197}.
FT   REGION      208    209       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00197}.
FT   ACT_SITE     70     70       {ECO:0000256|PROSITE-ProRule:PRU10125}.
FT   ACT_SITE     70     70       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   BINDING      11     11       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   BINDING      44     44       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   BINDING      61     61       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   BINDING     147    147       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   BINDING     180    180       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   SITE        149    149       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        198    198       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;  28997 MW;  5658427419D61B6C CRC64;
     MTFMKMHGLG NDFVVVDARL HPVRITGALA RGIAHRHLGV GFDQLAVIEP GKGDAHLVFY
     NADGSTSAAC GNATRCIARH LMDETGKTEL HLTTDRGDLY ARDAGDGLTS VNMGAPQLLW
     HEIPLAEEMD TLELPIEGGP TATGMGNPHC TFFVADAEAI PLAEFGARYE HHPLYPQRTN
     LQVAQITGPD RIRMRVWERG VGITLASGSS SCATAVAAAR RGLTGRKVQI DLDGGTIWID
     WREDGVWMTG PTMHVFSATL TPEFLASLG
//

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