MURQ2_VIBCH
ID MURQ2_VIBCH Reviewed; 307 AA.
AC Q9KU39;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=N-acetylmuramic acid 6-phosphate etherase 2 {ECO:0000255|HAMAP-Rule:MF_00068};
DE Short=MurNAc-6-P etherase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00068};
DE AltName: Full=N-acetylmuramic acid 6-phosphate lyase 2 {ECO:0000255|HAMAP-Rule:MF_00068};
GN Name=murQ2 {ECO:0000255|HAMAP-Rule:MF_00068}; OrderedLocusNames=VC_0690;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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: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; 1,6-anhydro-N-acetylmuramate
CC degradation. {ECO:0000255|HAMAP-Rule:MF_00068}.
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylmuramate degradation.
CC {ECO:0000255|HAMAP-Rule:MF_00068}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
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}.
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DR EMBL; AE003852; AAF93855.1; -; Genomic_DNA.
DR PIR; G82291; G82291.
DR RefSeq; NP_230339.1; NC_002505.1.
DR RefSeq; WP_000180252.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KU39; -.
DR SMR; Q9KU39; -.
DR STRING; 243277.VC_0690; -.
DR DNASU; 2615479; -.
DR EnsemblBacteria; AAF93855; AAF93855; VC_0690.
DR GeneID; 57989225; -.
DR KEGG; vch:VC_0690; -.
DR PATRIC; fig|243277.26.peg.661; -.
DR eggNOG; COG2103; Bacteria.
DR HOGENOM; CLU_049049_1_1_6; -.
DR OMA; TRNPATM; -.
DR BioCyc; VCHO:VC0690-MON; -.
DR UniPathway; UPA00342; -.
DR UniPathway; UPA00343; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0016835; F:carbon-oxygen lyase activity; IBA:GO_Central.
DR GO; GO:0016803; F:ether hydrolase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..307
FT /note="N-acetylmuramic acid 6-phosphate etherase 2"
FT /id="PRO_0000214842"
FT DOMAIN 62..225
FT /note="SIS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
FT ACT_SITE 90
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
FT ACT_SITE 121
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
SQ SEQUENCE 307 AA; 32730 MW; CF4F4790BB9C5EA6 CRC64;
MTNDALIAAL SHLVSEGRNP DTMDIDLLSS QEIVERLNQQ DKQVPLAVEA VLPQIAQAVD
KITAAFKQGG RLIYLGAGTS GRLGVLDASE CPPTFGVSDQ MVIGLIAGGK EAMFTAQEGA
EDNATLGAHD LQQIDFSSKD VLVGIAASGR TPYVIGALEY ANDLGATTIA LSCNPDSPIA
EIAQIAISPV VGPEALTGST RLKSGTAQKL VLNMLTTASM IRLGKSYQNL MVDVRATNRK
LIARAVRIVM QATDCQREEA EALLKESHNN AKLAILMHLT GMNYEQATAK LSQSDGFLRR
AMEEHEE
