(data stored in ACNUC7421 zone)

SWISSPROT: Q2ING7_ANADE

ID   Q2ING7_ANADE            Unreviewed;       266 AA.
AC   Q2ING7;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 93.
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   OrderedLocusNames=Adeh_0570 {ECO:0000313|EMBL:ABC80346.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC80346.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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: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; CP000251; ABC80346.1; -; Genomic_DNA.
DR   RefSeq; WP_011419629.1; NC_007760.1.
DR   STRING; 290397.Adeh_0570; -.
DR   EnsemblBacteria; ABC80346; ABC80346; Adeh_0570.
DR   KEGG; ade:Adeh_0570; -.
DR   eggNOG; ENOG4105E4Z; Bacteria.
DR   eggNOG; COG0253; LUCA.
DR   HOGENOM; HOG000220467; -.
DR   KO; K01778; -.
DR   OMA; MCGNGGR; -.
DR   BioCyc; ADEH290397:G1G5W-586-MONOMER; -.
DR   UniPathway; UPA00034; UER00025.
DR   Proteomes; UP000001935; 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; Q2ING7.
DR   SWISS-2DPAGE; Q2ING7.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197,
KW   ECO:0000256|SAAS:SAAS00028064};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
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:ABC80346.1};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197,
KW   ECO:0000256|SAAS:SAAS00028058};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935}.
FT   REGION       76     77       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     75     75       {ECO:0000256|PROSITE-ProRule:PRU10125}.
FT   ACT_SITE     75     75       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   ACT_SITE    207    207       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   BINDING      17     17       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   BINDING      66     66       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   BINDING     151    151       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   BINDING     181    181       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   SITE        153    153       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   266 AA;  27396 MW;  04CCF92473CD3FB6 CRC64;
     MMRRVPLPFV KYHGLGNDFV VVDGPLMDAA RARRICDRRR GVGADGVLTV LPPRTAGAAA
     TMHIFNSDGS VAAMCGNGIR CVARHLADAR GLDGDLVLDT DSGPKRCTIH RGPGGAVEAV
     SVEMGPARLE GEQEYRVGGE ALRALRVSMG NPHAVLFDAP ERARALAVGP ELERLVPGGV
     NVGFARPGPS GIDLVVWERG AGLTDACGTG ACAAAVASVS RGLARAGVPV EVRLPGGALA
     ITVAPDLVGV TMRGPAERAF TGETDL
//

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