ID Q72AX3_DESVH Unreviewed; 282 AA.
AC Q72AX3;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 01-MAY-2013, entry version 70.
DE RecName: Full=Diaminopimelate epimerase;
DE Short=DAP epimerase;
DE EC=5.1.1.7;
GN Name=dapF; OrderedLocusNames=DVU_1867;
OS Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB
OS 8303).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hildenborough / ATCC 29579 / NCIMB 8303;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N., Methe B., Brinkac L.M.,
RA Daugherty S.C., Deboy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D.,
RA Dimitrov G., Hance M., Tran K., Khouri H., Gill J., Utterback T.R.,
RA Feldblyum T.V., Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
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; AE017285; AAS96343.1; -; Genomic_DNA.
DR RefSeq; YP_011084.1; NC_002937.3.
DR ProteinModelPortal; Q72AX3; -.
DR STRING; 882.DVU1867; -.
DR EnsemblBacteria; AAS96343; AAS96343; DVU_1867.
DR GeneID; 2794311; -.
DR KEGG; dvu:DVU1867; -.
DR PATRIC; 32063474; VBIDesVul119526_1710.
DR eggNOG; COG0253; -.
DR KO; K01778; -.
DR OMA; VPHLVGF; -.
DR ProtClustDB; PRK00450; -.
DR BioCyc; DVUL882:GJIL-1910-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; Reference proteome.
FT REGION 83 85 Substrate binding (By similarity).
FT REGION 208 209 Substrate binding (By similarity).
FT REGION 219 220 Substrate binding (By similarity).
FT ACT_SITE 83 83 Proton donor/acceptor (By similarity).
FT ACT_SITE 218 218 Proton donor/acceptor (By similarity).
FT BINDING 18 18 Substrate (By similarity).
FT BINDING 53 53 Substrate (By similarity).
FT BINDING 74 74 Substrate (By similarity).
FT BINDING 190 190 Substrate (By similarity).
FT SITE 158 158 Important for catalytic activity (By
FT similarity).
FT SITE 208 208 Important for catalytic activity (By
FT similarity).
FT DISULFID 83 218 Size: 249-333 (By similarity).
SQ SEQUENCE 282 AA; 29964 MW; FC53A0F1844E88E4 CRC64;
MSGKKATVPF HKLHGCGNDF VFIDNRHLKL SVEAMPDWAR SICRRAFGVG ADGLVFLDTA
PQGHEADYIW HFYNADGSRA EMCGNASRCA AVLAVDLGFA GPRHAFGTDA GIVHAVADVE
AGYAKVELTR PRDLAAGTTL ELEGTPFTVH FVNTGVPHAV VFSDSVDGLD LRRLGAALRY
HPHFSPAGTN ANFASIIDRR TIHLRTYERG VEDETYACGT GAAATAFIAH TLGLTDASVG
VRTSGGEVLG IDIEDGSIFL SGKAVRVFSG EMHPEGLGLT LP
//
