(data stored in ACNUC7421 zone)

SWISSPROT: A0LEA8_SYNFM

ID   A0LEA8_SYNFM            Unreviewed;       287 AA.
AC   A0LEA8;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 88.
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=Sfum_0057 {ECO:0000313|EMBL:ABK15760.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK15760.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK15760.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-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; CP000478; ABK15760.1; -; Genomic_DNA.
DR   RefSeq; WP_011696933.1; NC_008554.1.
DR   STRING; 335543.Sfum_0057; -.
DR   EnsemblBacteria; ABK15760; ABK15760; Sfum_0057.
DR   KEGG; sfu:Sfum_0057; -.
DR   eggNOG; ENOG4105E4Z; Bacteria.
DR   eggNOG; COG0253; LUCA.
DR   HOGENOM; HOG000220466; -.
DR   KO; K01778; -.
DR   OMA; MCGNGGR; -.
DR   OrthoDB; 1921631at2; -.
DR   BioCyc; SFUM335543:G1G7I-59-MONOMER; -.
DR   UniPathway; UPA00034; UER00025.
DR   Proteomes; UP000001784; 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; A0LEA8.
DR   SWISS-2DPAGE; A0LEA8.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197,
KW   ECO:0000256|SAAS:SAAS00028064};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
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:ABK15760.1};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197,
KW   ECO:0000256|SAAS:SAAS00028058};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784}.
FT   REGION       81     82       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00197}.
FT   REGION      207    208       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00197}.
FT   REGION      218    219       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00197}.
FT   ACT_SITE     80     80       {ECO:0000256|PROSITE-ProRule:PRU10125}.
FT   ACT_SITE     80     80       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   ACT_SITE    217    217       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   BINDING      18     18       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   BINDING      71     71       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   BINDING     189    189       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   SITE        154    154       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        207    207       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   287 AA;  32106 MW;  4C8D2C7289B15C7D CRC64;
     MPVENERTRF LKMTGSGNDF IVLDNRAQGI SPEQGRELAR LACRRKLSVG ADGLILIEND
     PEVDFRWRFF NADGSEAEMC GNGARCAARF AHIKGIVAKS RMSFRTLAGI IEAEIKEPRV
     KIRMTPPHGL EPDLNVEAEQ RSFRLHFINT GVPHVVCFLE NDRALEEMNV FHWGRLLRHH
     RRFQPAGSNV NFALVEDANH MAIRTYERGV EDETLACGTG SIASALVAAA KGMVQSPVEV
     RTRSGETLTI YFDNPSTGAA AEFSQVYLEG DAKVVYEAEL WKETLRE
//

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