(data stored in ACNUC7421 zone)

SWISSPROT: DAPF_METNO

ID   DAPF_METNO              Reviewed;         293 AA.
AC   B8I9H6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 50.
DE   RecName: Full=Diaminopimelate epimerase {ECO:0000255|HAMAP-Rule:MF_00197};
DE            Short=DAP epimerase {ECO:0000255|HAMAP-Rule:MF_00197};
DE            EC=5.1.1.7 {ECO:0000255|HAMAP-Rule:MF_00197};
DE   AltName: Full=PLP-independent amino acid racemase {ECO:0000255|HAMAP-Rule:MF_00197};
GN   Name=dapF {ECO:0000255|HAMAP-Rule:MF_00197};
GN   OrderedLocusNames=Mnod_0183;
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_00197}.
CC   -!- CATALYTIC ACTIVITY: LL-2,6-diaminoheptanedioate = meso-
CC       diaminoheptanedioate. {ECO:0000255|HAMAP-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
CC       1/1. {ECO:0000255|HAMAP-Rule:MF_00197}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00197}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00197}.
CC   -!- SIMILARITY: Belongs to the diaminopimelate epimerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00197}.
DR   EMBL; CP001349; ACL55229.1; -; Genomic_DNA.
DR   RefSeq; WP_015926942.1; NC_011894.1.
DR   ProteinModelPortal; B8I9H6; -.
DR   SMR; B8I9H6; -.
DR   STRING; 460265.Mnod_0183; -.
DR   EnsemblBacteria; ACL55229; ACL55229; Mnod_0183.
DR   KEGG; mno:Mnod_0183; -.
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; UP000008207; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
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; B8I9H6.
DR   SWISS-2DPAGE; B8I9H6.
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; Isomerase;
KW   Lysine biosynthesis; Reference proteome.
FT   CHAIN         1    293       Diaminopimelate epimerase.
FT                                /FTId=PRO_1000124425.
FT   REGION       79     80       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   REGION      221    222       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   REGION      231    232       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   ACT_SITE     78     78       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   ACT_SITE    230    230       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING      17     17       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING      49     49       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING      69     69       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING     169    169       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING     203    203       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   SITE        171    171       Could be important to modulate the pK
FT                                values of the two catalytic cysteine
FT                                residues. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   SITE        221    221       Could be important to modulate the pK
FT                                values of the two catalytic cysteine
FT                                residues. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
SQ   SEQUENCE   293 AA;  31629 MW;  8F57AA6895E459E4 CRC64;
     MSPLAHRRFL KMNGLGNEIV VLDLRGTPHI VQPQEARAIA ADPRSRFDQL MVLHDPVTAG
     TDAALRIYNT DGSESGACGN GTRCVAWAML EDPVMGRPAE RLTLQSRAGL LAVTRVSATD
     FTVDMGPPRL RWDEIPLAEP FPDTRRIELQ IGPIDDPILH SPGVVSMGNP HAVFFVDRDP
     ASYDLARIGP LLEAHPIFPE RANISVAQVR GPEHIVLRVW ERGAGLTRAC GSAACAALVA
     AARLRLTGRR AVVTLPGGDL VIDWGEDDHV RMTGPTELEW EGTLAPSLFA GAA
//

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