ID A0A1R0FQH9_CITBR Unreviewed; 274 AA. AC A0A1R0FQH9; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 16-JAN-2019, entry version 7. 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 ORFNames=BWD41_23060 {ECO:0000313|EMBL:OLY66930.1}; OS Citrobacter braakii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex. OX NCBI_TaxID=57706 {ECO:0000313|EMBL:OLY66930.1, ECO:0000313|Proteomes:UP000185597}; RN [1] {ECO:0000313|EMBL:OLY66930.1, ECO:0000313|Proteomes:UP000185597} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCC4 {ECO:0000313|EMBL:OLY66930.1, RC ECO:0000313|Proteomes:UP000185597}; RA Liu J., Yang Y., Li Y., Liu D., Tuo H., Davis M., Zhang A.; RT "First report of the plasmid-mediated mcr-1 gene in Citrobacter RT freudii."; RL Submitted (JAN-2017) 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: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OLY66930.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MTCP01000016; OLY66930.1; -; Genomic_DNA. DR RefSeq; WP_016155126.1; NZ_PQWA01000008.1. DR UniPathway; UPA00034; UER00025. DR Proteomes; UP000185597; Unassembled WGS sequence. 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; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197, KW ECO:0000256|SAAS:SAAS00028064}; KW Complete proteome {ECO:0000313|Proteomes:UP000185597}; 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}; KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197, KW ECO:0000256|SAAS:SAAS00028058}. FT REGION 74 75 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00197}. FT REGION 208 209 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 73 73 {ECO:0000256|PROSITE-ProRule:PRU10125}. FT ACT_SITE 73 73 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 11 11 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00197}. FT BINDING 44 44 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00197}. FT BINDING 64 64 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00197}. FT BINDING 157 157 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00197}. FT BINDING 190 190 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00197}. FT SITE 159 159 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 208 208 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 268 268 Important for dimerization. FT {ECO:0000256|HAMAP-Rule:MF_00197}. SQ SEQUENCE 274 AA; 30312 MW; 01504554AED47A95 CRC64; MQFSKMHGLG NDFMVVDAVT QNVFFSPELI RRLSDRHLGV GFDQLLVVEP PYDPELDFHY RIFNADGSEV SQCGNGARCF ARFVRLKGLT NKRDIRVSTA NGRMVLTVTD DELVRVNMGE PNFEPAQVPF RANKAEKTYI MRVAEQTVLC GVVSMGNPHC VIQVDDVDTA TVETLGPVLE SHERFPERAN IGFMQVVKRE HIRLRVYERG AGETQACGSG ACAAVAVGIQ QGLLAEEVRV ELPGGRLDIA WKGPGHPLYM TGPAAHVYDG FIHL //