ID A0A0B7JF61_9GAMM Unreviewed; 301 AA. AC A0A0B7JF61; A0A2T3KD96; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 22-FEB-2023, entry version 33. DE RecName: Full=N-acetylmuramic acid 6-phosphate etherase {ECO:0000256|HAMAP-Rule:MF_00068}; DE Short=MurNAc-6-P etherase {ECO:0000256|HAMAP-Rule:MF_00068}; DE EC=4.2.1.126 {ECO:0000256|HAMAP-Rule:MF_00068}; 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 ECO:0000313|EMBL:PSU94311.1}; GN ORFNames=C9J27_19750 {ECO:0000313|EMBL:PSU94311.1}, PPBDW_II1087 GN {ECO:0000313|EMBL:CEO41756.1}; OS Photobacterium kishitanii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Photobacterium. OX NCBI_TaxID=318456 {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=ANT-2200 {ECO:0000313|EMBL:CEO41756.1}, and ANT220 RC {ECO:0000313|Proteomes:UP000019762}; RA Genoscope - CEA; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:PSU94311.1, ECO:0000313|Proteomes:UP000241426} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FS-7.2 {ECO:0000313|EMBL:PSU94311.1, RC ECO:0000313|Proteomes:UP000241426}; RA Butler K.; RT "Whole genome sequencing of Histamine producing bacteria."; RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Specifically catalyzes the cleavage of the D-lactyl ether CC substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D- CC lactate. Together with AnmK, is also required for the utilization of CC anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the CC medium or derived from its own cell wall murein, and thus plays a role CC in cell wall recycling. {ECO:0000256|HAMAP-Rule:MF_00068}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-acetyl-D-muramate 6-phosphate = (R)-lactate + N- CC acetyl-D-glucosamine 6-phosphate; Xref=Rhea:RHEA:26410, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16004, ChEBI:CHEBI:57513, CC ChEBI:CHEBI:58722; EC=4.2.1.126; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00068}; 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}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling. CC {ECO:0000256|HAMAP-Rule:MF_00068}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00068}. 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 aldehyde CC intermediate with (E)-stereochemistry, followed by the syn addition of CC water to give product. {ECO:0000256|HAMAP-Rule:MF_00068}. CC -!- SIMILARITY: Belongs to the GCKR-like family. MurNAc-6-P etherase CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00068}. 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: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 EMBL; PYNF01000024; PSU94311.1; -; Genomic_DNA. DR RefSeq; WP_036792186.1; NZ_LN794353.1. DR AlphaFoldDB; A0A0B7JF61; -. DR STRING; 1454202.PPBDW_100204___1; -. DR EnsemblBacteria; CEO41756; CEO41756; PPBDW_II1087. DR EnsemblBacteria; PSU94311; PSU94311; C9J27_19750. DR GeneID; 29945884; -. DR eggNOG; COG2103; Bacteria. DR UniPathway; UPA00342; -. DR UniPathway; UPA00343; -. DR UniPathway; UPA00544; -. DR Proteomes; UP000019762; Unassembled WGS sequence. DR Proteomes; UP000241426; Unassembled WGS sequence. DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro. DR GO; GO:0016835; F:carbon-oxygen lyase activity; IEA:UniProtKB-UniRule. 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-KW. DR GO; GO:0097173; P:N-acetylmuramic acid catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule. DR CDD; cd05007; SIS_Etherase; 1. DR Gene3D; 1.10.8.1080; -; 1. DR HAMAP; MF_00068; MurQ; 1. DR InterPro; IPR005488; Etherase_MurQ. DR InterPro; IPR005486; Glucokinase_regulatory_CS. DR InterPro; IPR040190; MURQ/GCKR. DR InterPro; IPR001347; SIS_dom. DR InterPro; IPR046348; SIS_dom_sf. DR PANTHER; PTHR10088; GLUCOKINASE REGULATORY PROTEIN; 1. DR PANTHER; PTHR10088:SF4; GLUCOKINASE REGULATORY PROTEIN; 1. DR Pfam; PF13580; SIS_2; 1. DR SUPFAM; SSF53697; SIS domain; 1. DR TIGRFAMs; TIGR00274; N-acetylmuramic acid 6-phosphate etherase; 1. DR PROSITE; PS01272; GCKR; 1. DR PROSITE; PS51464; SIS; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP- KW Rule:MF_00068}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00068}. FT DOMAIN 57..220 FT /note="SIS" FT /evidence="ECO:0000259|PROSITE:PS51464" FT ACT_SITE 85 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00068" FT ACT_SITE 116 FT /evidence="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 //