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Database: UniProt
Entry: B0TJ49_SHEHH
LinkDB: B0TJ49_SHEHH
Original site: B0TJ49_SHEHH 
ID   B0TJ49_SHEHH            Unreviewed;       286 AA.
AC   B0TJ49;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 97.
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   OrderedLocusNames=Shal_3912 {ECO:0000313|EMBL:ABZ78452.1};
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817 {ECO:0000313|EMBL:ABZ78452.1, ECO:0000313|Proteomes:UP000001317};
RN   [1] {ECO:0000313|EMBL:ABZ78452.1, ECO:0000313|Proteomes:UP000001317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB4 {ECO:0000313|EMBL:ABZ78452.1,
RC   ECO:0000313|Proteomes:UP000001317};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) 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; CP000931; ABZ78452.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0TJ49; -.
DR   STRING; 458817.Shal_3912; -.
DR   KEGG; shl:Shal_3912; -.
DR   eggNOG; COG0253; Bacteria.
DR   HOGENOM; CLU_053306_1_1_6; -.
DR   OMA; HVAMRVH; -.
DR   UniPathway; UPA00034; UER00025.
DR   Proteomes; UP000001317; 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        85
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10125"
FT   ACT_SITE        85
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   ACT_SITE        229
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         86..87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         220..221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         230..231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   SITE            171
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            220
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            280
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
SQ   SEQUENCE   286 AA;  31430 MW;  DEA396565EBB9879 CRC64;
     MRYRYFLRMS TLIQFTKMHG LGNDFMVVDG VTQNVFFSPD QIKRLADRNF GVGFDQLLLV
     EPPYDPDLDF HYRIFNADGS EVEQCGNGAR CFARFVRNKG LTHKHKIRVS TSSGKITLRL
     ERDGKVTVNM GIPVLEPSKI PFTAKKVEKT YLLLASSGTY LCGAVSMGNP HCVIEVDDVA
     AADVDTIGAE LTNHERFPKG VNVGFMQVVN SGHIKLRVYE RGAAETLACG TGACAAVVVG
     IQQGKLDRNV CVDLPGGSLM INWDGEGKPL WMTGPAEHVY DGQIAQ
//
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