ID A0A0M2UQP3_9BACT Unreviewed; 281 AA. AC A0A0M2UQP3; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 11-DEC-2019, entry version 18. 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=BROFUL_03140 {ECO:0000313|EMBL:KKO18187.1}; OS Candidatus Brocadia fulgida. OC Bacteria; Planctomycetes; Candidatus Brocadiae; Candidatus Brocadiales; OC Candidatus Brocadiaceae; Candidatus Brocadia. OX NCBI_TaxID=380242 {ECO:0000313|EMBL:KKO18187.1, ECO:0000313|Proteomes:UP000034954}; RN [1] {ECO:0000313|EMBL:KKO18187.1, ECO:0000313|Proteomes:UP000034954} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RU1 {ECO:0000313|EMBL:KKO18187.1}; RX PubMed=24267221; DOI=10.1186/1471-2180-13-265; RA Ferousi C., Speth D.R., Reimann J., Op den Camp H.J., Allen J.W., RA Keltjens J.T., Jetten M.S.; RT "Identification of the type II cytochrome c maturation pathway in anammox RT bacteria by comparative genomics."; RL BMC Microbiol. 13:265-265(2013). 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=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 1/1. CC {ECO:0000256|HAMAP-Rule:MF_00197, 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 of CC feature annotation. {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:KKO18187.1}. 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; LAQJ01000287; KKO18187.1; -; Genomic_DNA. DR PATRIC; fig|380242.3.peg.3873; -. DR UniPathway; UPA00034; UER00025. DR Proteomes; UP000034954; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197, ECO:0000256|SAAS:SAAS00028054}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00197, ECO:0000256|SAAS:SAAS00118214}; KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197, KW ECO:0000256|SAAS:SAAS00028058}; KW Reference proteome {ECO:0000313|Proteomes:UP000034954}. FT REGION 72..73 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT REGION 212..213 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT REGION 222..223 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT ACT_SITE 71 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10125" FT ACT_SITE 71 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT ACT_SITE 221 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 62 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT BINDING 161 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT BINDING 194 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT SITE 163 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 212 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" SQ SEQUENCE 281 AA; 30715 MW; 20A0104C09787A87 CRC64; MKFTKMHGIG NDYVYINCFE EEIGVPAKLA PIISDRHFGV GSDGLILILS SAVADCRMRI FNADGSEAQM CGNGIRCVAK YVYDNKITQK NPLTVETLAG IKTVQVFTEN GRVSKARVNM GKPGLMRSEI PMIGNETKVI DESLPIDKNV SFRITCVSMG NPHCVVFVDD LDGLDISKYG PEIERHRVFP ERINVHFVRI HNPKEVTMKT WERGSGITMA CGTGASAVCV AGVLNKKTER NVLAHLPGGD LELEWAADGN VYMTGPATEV FTGEGTFTQK G //