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Database: UniProt
Entry: H3RIW1_PANSE
LinkDB: H3RIW1_PANSE
Original site: H3RIW1_PANSE 
ID   H3RIW1_PANSE            Unreviewed;       274 AA.
AC   H3RIW1;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Diaminopimelate epimerase {ECO:0000256|ARBA:ARBA00013080, ECO:0000256|HAMAP-Rule:MF_00197};
DE            Short=DAP epimerase {ECO:0000256|HAMAP-Rule:MF_00197};
DE            EC=5.1.1.7 {ECO:0000256|ARBA:ARBA00013080, ECO:0000256|HAMAP-Rule:MF_00197};
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:EHT98645.1};
GN   ORFNames=CKS_4438 {ECO:0000313|EMBL:EHT98645.1}, DSJ_22085
GN   {ECO:0000313|EMBL:ARF52034.1};
OS   Pantoea stewartii subsp. stewartii DC283.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=660596 {ECO:0000313|EMBL:EHT98645.1, ECO:0000313|Proteomes:UP000005050};
RN   [1] {ECO:0000313|EMBL:EHT98645.1, ECO:0000313|Proteomes:UP000005050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DC283 {ECO:0000313|EMBL:EHT98645.1,
RC   ECO:0000313|Proteomes:UP000005050};
RX   PubMed=22111898; DOI=10.1111/j.1365-2958.2011.07926.x;
RA   Wang X., Yang F., von Bodman S.B.;
RT   "The genetic and structural basis of two distinct terminal side branch
RT   residues in stewartan and amylovoran exopolysaccharides and their potential
RT   role in host adaptation.";
RL   Mol. Microbiol. 83:195-207(2012).
RN   [2] {ECO:0000313|EMBL:EHT98645.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DC283 {ECO:0000313|EMBL:EHT98645.1};
RA   Biehl B.S., Ding Y., Dugan-Rocha S.P., Gibbs R.A., Glasner J.D., Kovar C.,
RA   Muzny D.M., Neeno-Eckwall E.C., Perna N.T., Qin X., von Bodman S.B.,
RA   Weinstock G.M.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ARF52034.1, ECO:0000313|Proteomes:UP000192380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DC283 {ECO:0000313|EMBL:ARF52034.1,
RC   ECO:0000313|Proteomes:UP000192380};
RA   Duong D.A., Stevens A.M., Jensen R.V.;
RT   "Complete Genome Assembly of Pantoea stewartii subsp. stewartii DC283, a
RT   Corn Pathogen.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate
CC       (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-
CC       lysine and an essential component of the bacterial peptidoglycan.
CC       {ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,6S)-2,6-diaminoheptanedioate = meso-2,6-
CC         diaminoheptanedioate; Xref=Rhea:RHEA:15393, ChEBI:CHEBI:57609,
CC         ChEBI:CHEBI:57791; EC=5.1.1.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00000599, ECO:0000256|HAMAP-
CC         Rule:MF_00197};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005196, ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- SIMILARITY: Belongs to the diaminopimelate epimerase family.
CC       {ECO:0000256|ARBA:ARBA00010219, ECO:0000256|HAMAP-Rule:MF_00197}.
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DR   EMBL; CP017581; ARF52034.1; -; Genomic_DNA.
DR   EMBL; AHIE01000034; EHT98645.1; -; Genomic_DNA.
DR   RefSeq; WP_006121449.1; NZ_CP017581.1.
DR   AlphaFoldDB; H3RIW1; -.
DR   STRING; 660596.DSJ_22085; -.
DR   KEGG; pstw:DSJ_22085; -.
DR   PATRIC; fig|660596.6.peg.4231; -.
DR   eggNOG; COG0253; Bacteria.
DR   OrthoDB; 9805408at2; -.
DR   UniPathway; UPA00034; UER00025.
DR   Proteomes; UP000005050; Unassembled WGS sequence.
DR   Proteomes; UP000192380; 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   NCBIfam; TIGR00652; DapF; 1.
DR   PANTHER; PTHR31689:SF0; DIAMINOPIMELATE EPIMERASE; 1.
DR   PANTHER; PTHR31689; DIAMINOPIMELATE EPIMERASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01678; DAP_epimerase; 2.
DR   SUPFAM; SSF54506; Diaminopimelate epimerase-like; 1.
DR   PROSITE; PS01326; DAP_EPIMERASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00197}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00197};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP-
KW   Rule:MF_00197}.
FT   ACT_SITE        73
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10125"
FT   ACT_SITE        73
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   ACT_SITE        217
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         74..75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         208..209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         218..219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   SITE            159
FT                   /note="Could be important to modulate the pK values of the
FT                   two catalytic cysteine residues"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   SITE            208
FT                   /note="Could be important to modulate the pK values of the
FT                   two catalytic cysteine residues"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   SITE            268
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
SQ   SEQUENCE   274 AA;  30219 MW;  D0C6E9473374F328 CRC64;
     MQFSKMHGLG NDFMVVDAVT QNVFFSPELI RRLADRHLGV GFDQLLIVEP PYDPDLDFHY
     RIFNADGSEV AQCGNGARCF ARFVQLKGLT NKSDIRVSTQ AGRMVLSVTP DELVRVNMGE
     PNFEPHQVPF RANKAENLYL LRVAEQTVMF GAVSMGNPHC VIQVESTKTA QVELLGPILE
     SHERFPERVN VGFMEIINPE HIRLRVYERG AGETQACGSG ACAAVACGIQ QGILSQKVRV
     DLPGGTLHIA WKGAGQPLFM TGPATHVYDG FIHL
//
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