(data stored in ACNUC7421 zone)

SWISSPROT: MURQ_AERHH

ID   MURQ_AERHH              Reviewed;         298 AA.
AC   A0KFC0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 81.
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=AHA_0413;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240;
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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:0000255|HAMAP-
CC       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
CC       aldehyde intermediate with (E)-stereochemistry, followed by the
CC       syn addition of water to give product. {ECO:0000255|HAMAP-
CC       Rule:MF_00068}.
CC   -!- SIMILARITY: Belongs to the GCKR-like family. MurNAc-6-P etherase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00068}.
DR   EMBL; CP000462; ABK36652.1; -; Genomic_DNA.
DR   RefSeq; WP_011704387.1; NC_008570.1.
DR   RefSeq; YP_854942.1; NC_008570.1.
DR   SMR; A0KFC0; -.
DR   STRING; 380703.AHA_0413; -.
DR   EnsemblBacteria; ABK36652; ABK36652; AHA_0413.
DR   GeneID; 4487211; -.
DR   KEGG; aha:AHA_0413; -.
DR   PATRIC; fig|380703.7.peg.402; -.
DR   eggNOG; ENOG4105E15; Bacteria.
DR   eggNOG; COG2103; LUCA.
DR   HOGENOM; HOG000084045; -.
DR   KO; K07106; -.
DR   OMA; CPPTFCT; -.
DR   BioCyc; AHYD380703:G1G7B-414-MONOMER; -.
DR   UniPathway; UPA00342; -.
DR   UniPathway; UPA00343; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000000756; Chromosome.
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: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   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.
DR   PANTHER; PTHR10088; PTHR10088; 1.
DR   PANTHER; PTHR10088:SF5; PTHR10088:SF5; 1.
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;
DR   PRODOM; A0KFC0.
DR   SWISS-2DPAGE; A0KFC0.
KW   Carbohydrate metabolism; Complete proteome; Lyase; Reference proteome.
FT   CHAIN         1    298       N-acetylmuramic acid 6-phosphate
FT                                etherase.
FT                                /FTId=PRO_1000009108.
FT   DOMAIN       57    220       SIS. {ECO:0000255|HAMAP-Rule:MF_00068}.
FT   ACT_SITE     85     85       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00068}.
FT   ACT_SITE    116    116       {ECO:0000255|HAMAP-Rule:MF_00068}.
SQ   SEQUENCE   298 AA;  31118 MW;  D58A72957E30D872 CRC64;
     MTIDLSSMIT ETRNPASVEI DQLPTLEMLR VINQEDQQVA LAVSQLLPEI TRAVDAIAAA
     FGKGGRLVYI GAGTSGRLGI LDASECPPTY GVSAEQVVGL IAGGHKAILQ AVENAEDDAE
     LGAQDLKNIQ FCANDVLVGI AASGRTPYVL GAMAHARAVG ATVCSISCNP GSPLAQAADI
     SMVAVVGPEI VTGSSRMKAG TAQKLILNML STGAMIRTGK VYGNLMVDVE ATNAKLVERQ
     KRIVMEATDC ERAVAERALA QADNHCKTAI VMILAGLTAD EARTRLQSSN GFISQCTH
//

If you have problems or comments...

PBIL Back to PBIL home page