MURQ_SYNE7
ID MURQ_SYNE7 Reviewed; 307 AA.
AC O33701; Q31K12;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=N-acetylmuramic acid 6-phosphate etherase {ECO:0000255|HAMAP-Rule:MF_00068};
DE Short=MurNAc-6-P etherase {ECO:0000255|HAMAP-Rule:MF_00068};
DE EC=4.2.1.126 {ECO:0000255|HAMAP-Rule:MF_00068};
DE AltName: Full=N-acetylmuramic acid 6-phosphate hydrolase {ECO:0000255|HAMAP-Rule:MF_00068};
DE AltName: Full=N-acetylmuramic acid 6-phosphate lyase {ECO:0000255|HAMAP-Rule:MF_00068};
GN Name=murQ {ECO:0000255|HAMAP-Rule:MF_00068};
GN OrderedLocusNames=Synpcc7942_2577;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9240461; DOI=10.1006/bbrc.1997.6992;
RA Oguchi K., Nimura K., Yoshikawa H., Takahashi H.;
RT "Sequence and analysis of a dnaJ homologue gene in cyanobacterium
RT Synechococcus sp. PCC7942.";
RL Biochem. Biophys. Res. Commun. 236:461-466(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_00068};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylmuramate degradation.
CC {ECO:0000255|HAMAP-Rule:MF_00068}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00068}.
CC -!- SIMILARITY: Belongs to the GCKR-like family. MurNAc-6-P etherase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00068}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA21681.1; Type=Frameshift; Evidence={ECO:0000305};
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; AB003519; BAA21681.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP000100; ABB58607.1; -; Genomic_DNA.
DR PIR; JC5552; JC5552.
DR RefSeq; WP_011243843.1; NC_007604.1.
DR AlphaFoldDB; O33701; -.
DR SMR; O33701; -.
DR STRING; 1140.Synpcc7942_2577; -.
DR PRIDE; O33701; -.
DR EnsemblBacteria; ABB58607; ABB58607; Synpcc7942_2577.
DR KEGG; syf:Synpcc7942_2577; -.
DR eggNOG; COG2103; Bacteria.
DR HOGENOM; CLU_049049_1_1_3; -.
DR OMA; CPPTFCT; -.
DR OrthoDB; 1100044at2; -.
DR BioCyc; SYNEL:SYNPCC7942_2577-MON; -.
DR UniPathway; UPA00342; -.
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: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 CDD; cd05007; SIS_Etherase; 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; PTHR10088; 1.
DR PANTHER; PTHR10088:SF5; PTHR10088:SF5; 1.
DR Pfam; PF13580; SIS_2; 1.
DR SUPFAM; SSF53697; SSF53697; 1.
DR TIGRFAMs; TIGR00274; TIGR00274; 1.
DR PROSITE; PS01272; GCKR; 1.
DR PROSITE; PS51464; SIS; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Lyase.
FT CHAIN 1..307
FT /note="N-acetylmuramic acid 6-phosphate etherase"
FT /id="PRO_0000214838"
FT DOMAIN 60..223
FT /note="SIS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
FT ACT_SITE 88
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
FT ACT_SITE 119
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
SQ SEQUENCE 307 AA; 32231 MW; 6C5270D13D462EF1 CRC64;
MDPSLSDRGH LLTEQANPAS QALDQLSPLE LVDLFNQEDQ HCLAAVAQAR EAIAQAIEYA
AQAIARGGRL FYIGAGTSGR LGVLDAAECP PTFCSDPEQV QGILAGGSAA MFRSSEGLED
RAEDGAVAIA EYQIGPRDFI LGITAGGTTP YVHGALEAAR SAGAKTGFLA CVPADQVAIA
VDVDIRVPVG PEILAGSTRL KAGTVTKMVL NQISTGAMVR IGKVYGNRMV DVAVTNRKLE
DRALRILSDL LSIDRQQAAA LLGANERSVK QALLQHWTGL EPAEAAALLT EHQGHLRAAV
TAFSSLR
