ID F6GBW8_LACS5 Unreviewed; 259 AA.
AC F6GBW8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 03-APR-2013, entry version 10.
DE RecName: Full=Diaminopimelate epimerase;
DE Short=DAP epimerase;
DE EC=5.1.1.7;
GN Name=dapF; OrderedLocusNames=Lacal_0009;
OS Lacinutrix sp. (strain 5H-3-7-4).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lacinutrix.
OX NCBI_TaxID=983544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5H-3-7-4;
RX PubMed=21725025; DOI=10.1128/JB.05518-11;
RA Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C.,
RA Goodwin L.A., Han J., Han S., Hauser L., Land M.L., Nolan M.,
RA Ovchinnikova G., Pennacchio L., Pitluck S., Tapia R., Woyke T.,
RA Wiebusch S., Basner A., Abe F., Horikoshi K., Keller M.,
RA Antranikian G.;
RT "Complete genome sequences of Krokinobacter sp. strain 4H-3-7-5 and
RT Lacinutrix sp. strain 5H-3-7-4, polysaccharide-degrading members of
RT the family Flavobacteriaceae.";
RL J. Bacteriol. 193:4545-4546(2011).
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 (By similarity).
CC -!- CATALYTIC ACTIVITY: LL-2,6-diaminoheptanedioate = meso-
CC diaminoheptanedioate.
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the diaminopimelate epimerase family.
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DR EMBL; CP002825; AEG99861.1; -; Genomic_DNA.
DR RefSeq; YP_004578290.1; NC_015638.1.
DR EnsemblBacteria; AEG99861; AEG99861; Lacal_0009.
DR GeneID; 10777638; -.
DR KEGG; lan:Lacal_0009; -.
DR KO; K01778; -.
DR BioCyc; LSP983544:GHSZ-9-MONOMER; -.
DR UniPathway; UPA00034; UER00025.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:HAMAP.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:HAMAP.
DR HAMAP; MF_00197; DAP_epimerase; 1; -.
DR InterPro; IPR018510; DAP_epimerase_AS.
DR InterPro; IPR001653; DAP_epimerase_DapF.
DR Pfam; PF01678; DAP_epimerase; 2.
DR TIGRFAMs; TIGR00652; DapF; 1.
DR PROSITE; PS01326; DAP_EPIMERASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; Disulfide bond;
KW Isomerase; Lysine biosynthesis.
FT REGION 74 76 Substrate binding (By similarity).
FT REGION 188 189 Substrate binding (By similarity).
FT REGION 199 200 Substrate binding (By similarity).
FT ACT_SITE 74 74 Proton donor/acceptor (By similarity).
FT ACT_SITE 198 198 Proton donor/acceptor (By similarity).
FT BINDING 13 13 Substrate (By similarity).
FT BINDING 47 47 Substrate (By similarity).
FT BINDING 65 65 Substrate (By similarity).
FT BINDING 170 170 Substrate (By similarity).
FT SITE 138 138 Important for catalytic activity (By
FT similarity).
FT SITE 188 188 Important for catalytic activity (By
FT similarity).
FT DISULFID 74 198 Size: 249-333 (By similarity).
SQ SEQUENCE 259 AA; 28611 MW; 3B93EC237D282DA9 CRC64;
MTHTFYKYQG TGNDFVFIDN RQEQFNKNNT KLIAHLCDRR FGIGADGLIL LENDATADFK
MVYFNADGNE STMCGNGGRC IVAFAEKLNI INGKTTFNAI DGIHEATIND GFVKLKMQDV
DTIKVNKDHT FLNTGSPHHV ALVNNIKQFD VKTEGAAIRY GDLYDAAGTN VNFVEPLDNS
TFSVRTYERG VEDETLSCGT GVTAVALAMH TLKKANTQEV SLNVEGGTLK VSFEKTTNGY
KNIWLQGPAT LVFKGEIEW
//
