ID A0A1R0FQH9_CITBR Unreviewed; 274 AA. AC A0A1R0FQH9; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 19-JAN-2022, entry version 18. DE RecName: Full=Diaminopimelate epimerase {ECO:0000256|ARBA:ARBA00013080, ECO:0000256|HAMAP-Rule:MF_00197}; DE Short=DAP epimerase {ECO:0000256|HAMAP-Rule:MF_00197}; DE EC=5.1.1.7 {ECO:0000256|ARBA:ARBA00013080, ECO:0000256|HAMAP-Rule:MF_00197}; DE AltName: Full=PLP-independent amino acid racemase {ECO:0000256|HAMAP-Rule:MF_00197}; GN Name=dapF {ECO:0000256|HAMAP-Rule:MF_00197, GN ECO:0000313|EMBL:KAA0548972.1}; GN ORFNames=BWD41_23060 {ECO:0000313|EMBL:OLY66930.1}, EY919_14665 GN {ECO:0000313|EMBL:TCC71698.1}, F0327_23670 GN {ECO:0000313|EMBL:KAA0548972.1}; 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 freudii."; RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:TCC71698.1, ECO:0000313|Proteomes:UP000291251} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HH9 {ECO:0000313|EMBL:TCC71698.1, RC ECO:0000313|Proteomes:UP000291251}; RA Duceppe M.-O., Huang H.; RT "Genomic sequences of eight Citrobacter braakii and Citrobacter freundii RT strains."; RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:KAA0548972.1, ECO:0000313|Proteomes:UP000325014} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C7 {ECO:0000313|EMBL:KAA0548972.1, RC ECO:0000313|Proteomes:UP000325014}; RA Cho G.-S., Stein M., Fiedler G., Igbinosa E.O., Heuermann L., Brinks E., RA Neve H., Franz C.M.A.P.; RT "Characterization of antibiotic-resistant enterobacteria."; RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate CC (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- CC lysine and an essential component of the bacterial peptidoglycan. CC {ECO:0000256|HAMAP-Rule:MF_00197}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2S,6S)-2,6-diaminoheptanedioate = meso-2,6- CC diaminoheptanedioate; Xref=Rhea:RHEA:15393, ChEBI:CHEBI:57609, CC ChEBI:CHEBI:57791; EC=5.1.1.7; CC Evidence={ECO:0000256|ARBA:ARBA00000599, ECO:0000256|HAMAP- CC Rule:MF_00197}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1. CC {ECO:0000256|ARBA:ARBA00005196, ECO:0000256|HAMAP-Rule:MF_00197}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00197}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197}. CC -!- SIMILARITY: Belongs to the diaminopimelate epimerase family. CC {ECO:0000256|ARBA:ARBA00010219, ECO:0000256|HAMAP-Rule:MF_00197}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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; VTTU01000046; KAA0548972.1; -; Genomic_DNA. DR EMBL; MTCP01000016; OLY66930.1; -; Genomic_DNA. DR EMBL; SJSF01000012; TCC71698.1; -; Genomic_DNA. DR RefSeq; WP_016155126.1; NZ_WJGK01000011.1. DR EnsemblBacteria; OLY66930; OLY66930; BWD41_23060. DR GeneID; 66272096; -. DR UniPathway; UPA00034; UER00025. DR Proteomes; UP000185597; Unassembled WGS sequence. DR Proteomes; UP000291251; Unassembled WGS sequence. DR Proteomes; UP000325014; 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|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00197}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00197}; KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP- KW Rule:MF_00197}. FT REGION 74..75 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT REGION 208..209 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT REGION 218..219 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT ACT_SITE 73 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10125" FT ACT_SITE 73 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT ACT_SITE 217 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT BINDING 11 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT BINDING 44 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT BINDING 64 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT BINDING 157 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT BINDING 190 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT SITE 159 FT /note="Could be important to modulate the pK values of the FT two catalytic cysteine residues" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT SITE 208 FT /note="Could be important to modulate the pK values of the FT two catalytic cysteine residues" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT SITE 268 FT /note="Important for dimerization" FT /evidence="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 //