ID A0A0B7JF61_PHOPO Unreviewed; 301 AA. AC A0A0B7JF61; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 18-JAN-2017, entry version 14. DE RecName: Full=N-acetylmuramic acid 6-phosphate etherase {ECO:0000256|HAMAP-Rule:MF_00068, ECO:0000256|SAAS:SAAS00510861}; DE Short=MurNAc-6-P etherase {ECO:0000256|HAMAP-Rule:MF_00068}; DE EC=4.2.1.126 {ECO:0000256|HAMAP-Rule:MF_00068, ECO:0000256|SAAS:SAAS00510861}; DE AltName: Full=N-acetylmuramic acid 6-phosphate hydrolase {ECO:0000256|HAMAP-Rule:MF_00068}; DE AltName: Full=N-acetylmuramic acid 6-phosphate lyase {ECO:0000256|HAMAP-Rule:MF_00068}; GN Name=yfeU {ECO:0000313|EMBL:CEO41756.1}; GN Synonyms=murQ {ECO:0000256|HAMAP-Rule:MF_00068}; GN ORFNames=PPBDW_II1087 {ECO:0000313|EMBL:CEO41756.1}; OS Photobacterium phosphoreum ANT-2200. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=1454202 {ECO:0000313|EMBL:CEO41756.1, ECO:0000313|Proteomes:UP000019762}; RN [1] {ECO:0000313|EMBL:CEO41756.1, ECO:0000313|Proteomes:UP000019762} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ANT220 {ECO:0000313|Proteomes:UP000019762}; RA Genoscope - CEA; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Specifically catalyzes the cleavage of the D-lactyl CC ether substituent of MurNAc 6-phosphate, producing GlcNAc 6- CC phosphate and D-lactate. Together with AnmK, is also required for CC the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either CC imported from the medium or derived from its own cell wall murein, CC and thus plays a role in cell wall recycling. {ECO:0000256|HAMAP- CC Rule:MF_00068}. CC -!- CATALYTIC ACTIVITY: (R)-lactate + N-acetyl-D-glucosamine 6- CC phosphate = N-acetylmuramate 6-phosphate + H(2)O. CC {ECO:0000256|HAMAP-Rule:MF_00068, ECO:0000256|SAAS:SAAS00510857}. CC -!- PATHWAY: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate CC degradation. {ECO:0000256|HAMAP-Rule:MF_00068}. CC -!- PATHWAY: Amino-sugar metabolism; N-acetylmuramate degradation. CC {ECO:0000256|HAMAP-Rule:MF_00068, ECO:0000256|SAAS:SAAS00510845}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling. CC {ECO:0000256|HAMAP-Rule:MF_00068}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00068, CC ECO:0000256|SAAS:SAAS00510849}. CC -!- MISCELLANEOUS: A lyase-type mechanism (elimination/hydration) is CC suggested for the cleavage of the lactyl ether bond of MurNAc 6- CC phosphate, with the formation of an alpha,beta-unsaturated CC aldehyde intermediate with (E)-stereochemistry, followed by the CC syn addition of water to give product. {ECO:0000256|HAMAP- CC Rule:MF_00068}. CC -!- SIMILARITY: Belongs to the GCKR-like family. MurNAc-6-P etherase CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00068, CC ECO:0000256|SAAS:SAAS00570217}. 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:CEO41756.1}. 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; CCAR020000009; CEO41756.1; -; Genomic_DNA. DR RefSeq; WP_036792186.1; NZ_LN794353.1. DR EnsemblBacteria; CEO41756; CEO41756; PPBDW_II1087. DR GeneID; 29946187; -. DR UniPathway; UPA00342; -. DR UniPathway; UPA00343; -. DR UniPathway; UPA00544; -. DR Proteomes; UP000019762; Unassembled WGS sequence. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016835; F:carbon-oxygen lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0097175; P:1,6-anhydro-N-acetyl-beta-muramic acid catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0046348; P:amino sugar catabolic process; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0097173; P:N-acetylmuramic acid catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-HAMAP. DR CDD; cd05007; SIS_Etherase; 1. DR HAMAP; MF_00068; MurQ; 1. DR InterPro; IPR005488; Etherase_MurQ. DR InterPro; IPR005486; Glucokinase_regulatory_CS. DR InterPro; IPR001347; SIS. DR Pfam; PF13580; SIS_2; 1. DR TIGRFAMs; TIGR00274; TIGR00274; 1. DR PROSITE; PS01272; GCKR; 1. DR PROSITE; PS51464; SIS; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00068, KW ECO:0000256|SAAS:SAAS00510852}; KW Complete proteome {ECO:0000313|Proteomes:UP000019762}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00068, KW ECO:0000256|SAAS:SAAS00510838}. FT DOMAIN 57 220 SIS. {ECO:0000259|PROSITE:PS51464}. FT ACT_SITE 85 85 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_00068}. FT ACT_SITE 116 116 {ECO:0000256|HAMAP-Rule:MF_00068}. SQ SEQUENCE 301 AA; 31358 MW; 8A6D252F15A0D7E3 CRC64; MKIDLTHLVT ESRNSASEAI DTLSTLDMLK VINDEDKKVA LAVEQTLPAI AQAVDAIAAA FQNGGRLVYV GAGTSGRLGI LDASECPPTY GSAPEQVVGL IAGGHQAILK AVENAEDNIE MGAEDLKAIN FSARDVLVGI AASGRTPYVL GAMAYARSVN AIVACVSCNP QSPMTAAADI VITPVVGAEV VTGSSRMKAG TAQKLVLNML TTGAMIRIGK IYGNLMVDVE ATNAKLVERQ KNIVMQATEC DRAQAEAALD ACNGHCKTAI VMILTGVNNV TAKTLLQQNN GYIRSAIAKN C //