(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BIW9_GEOS0

ID   A0A0F6BIW9_GEOS0        Unreviewed;       284 AA.
AC   A0A0F6BIW9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 25.
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=GY4MC1_0538 {ECO:0000313|EMBL:ADP73370.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73370.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73370.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73370.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) 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; CP002293; ADP73370.1; -; Genomic_DNA.
DR   RefSeq; WP_003248317.1; NC_014650.1.
DR   EnsemblBacteria; ADP73370; ADP73370; GY4MC1_0538.
DR   GeneID; 29236808; -.
DR   KEGG; gmc:GY4MC1_0538; -.
DR   KO; K01778; -.
DR   OMA; MCGNGGR; -.
DR   OrthoDB; 1921631at2; -.
DR   BioCyc; GSP581103:G1GOQ-588-MONOMER; -.
DR   UniPathway; UPA00034; UER00025.
DR   Proteomes; UP000002034; 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; A0A0F6BIW9.
DR   SWISS-2DPAGE; A0A0F6BIW9.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197,
KW   ECO:0000256|SAAS:SAAS00028064};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
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:ADP73370.1};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197,
KW   ECO:0000256|SAAS:SAAS00028058}.
FT   REGION       77     78       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00197}.
FT   REGION      217    218       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00197}.
FT   REGION      227    228       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00197}.
FT   ACT_SITE     76     76       {ECO:0000256|PROSITE-ProRule:PRU10125}.
FT   ACT_SITE     76     76       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   ACT_SITE    226    226       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   BINDING      14     14       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   BINDING      67     67       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   BINDING     166    166       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   BINDING     199    199       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00197}.
FT   SITE        168    168       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        217    217       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   284 AA;  30861 MW;  7EE2B1AC27007751 CRC64;
     MNQFSFTKMH GLGNSYIYVN MFEETIPESL LSLLAVKVSN VNTGIGADGM ILICPSKVAP
     VKMRIFNSDG SEGKNCGNGL RCVAKYVYEH GIVNDRSFFI ETLSGLVKAE VEVENGAVTN
     VTIDMGKPRL KRSEIPMVGP EAERVVAEPF EVDGQLYEIT AVSMGNPHVI FYVDDINQAA
     VTSLGPIVEK DKRFPEGVNV EFVEVVNDHE LHFRVWERGS GVTQACGTGA CAAVVASVLN
     GKTARNKETI VHLAGGDLTI TWTDEGNVRM TGPAETICTG VYYY
//

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