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-MAY-2016, entry version 5. DE RecName: Full=Diaminopimelate epimerase {ECO:0000256|HAMAP-Rule:MF_00197, ECO:0000256|SAAS:SAAS00316707}; 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:SAAS00316689}; 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; Planctomycetia; 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 RT anammox bacteria by comparative genomics."; RL BMC Microbiol. 13:265-265(2013). 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 ECO:0000256|SAAS:SAAS00351434}. CC -!- CATALYTIC ACTIVITY: LL-2,6-diaminoheptanedioate = meso- CC diaminoheptanedioate. {ECO:0000256|HAMAP-Rule:MF_00197, CC ECO:0000256|SAAS:SAAS00316693}. 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:SAAS00316687}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197, CC ECO:0000256|SAAS:SAAS00316708}. CC -!- SIMILARITY: Belongs to the diaminopimelate epimerase family. CC {ECO:0000256|HAMAP-Rule:MF_00197, ECO:0000256|SAAS:SAAS00583234}. 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: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 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-HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. 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:SAAS00429653}; KW Complete proteome {ECO:0000313|Proteomes:UP000034954}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197, KW ECO:0000256|SAAS:SAAS00429534}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00197, KW ECO:0000256|SAAS:SAAS00429665}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00197, KW ECO:0000256|SAAS:SAAS00475366}; KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197, KW ECO:0000256|SAAS:SAAS00429562}; KW Reference proteome {ECO:0000313|Proteomes:UP000034954}. FT REGION 8 9 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00197}. FT REGION 71 73 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00197}. FT REGION 212 213 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00197}. FT REGION 222 223 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00197}. FT ACT_SITE 71 71 Proton donor/acceptor. FT {ECO:0000256|HAMAP-Rule:MF_00197}. FT ACT_SITE 221 221 Proton donor/acceptor. FT {ECO:0000256|HAMAP-Rule: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 62 62 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00197}. FT BINDING 161 161 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00197}. FT BINDING 194 194 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00197}. FT SITE 163 163 Important for catalytic activity. FT {ECO:0000256|HAMAP-Rule:MF_00197}. FT SITE 212 212 Important for catalytic activity. FT {ECO:0000256|HAMAP-Rule:MF_00197}. FT DISULFID 71 221 {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 //