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Database: UniProt
Entry: K9W9Z8_9CYAN
LinkDB: K9W9Z8_9CYAN
Original site: K9W9Z8_9CYAN 
ID   K9W9Z8_9CYAN            Unreviewed;       310 AA.
AC   K9W9Z8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 57.
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=murQ {ECO:0000256|HAMAP-Rule:MF_00068};
GN   ORFNames=Mic7113_1330 {ECO:0000313|EMBL:AFZ17215.1};
OS   Allocoleopsis franciscana PCC 7113.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC   Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX   NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ17215.1, ECO:0000313|Proteomes:UP000010471};
RN   [1] {ECO:0000313|EMBL:AFZ17215.1, ECO:0000313|Proteomes:UP000010471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ17215.1,
RC   ECO:0000313|Proteomes:UP000010471};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Microcoleus sp. PCC 7113.";
RL   Submitted (JUN-2012) 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: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; N-acetylmuramate degradation.
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}.
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DR   EMBL; CP003630; AFZ17215.1; -; Genomic_DNA.
DR   RefSeq; WP_015181375.1; NC_019738.1.
DR   AlphaFoldDB; K9W9Z8; -.
DR   STRING; 1173027.Mic7113_1330; -.
DR   KEGG; mic:Mic7113_1330; -.
DR   PATRIC; fig|1173027.3.peg.1474; -.
DR   eggNOG; COG2103; Bacteria.
DR   HOGENOM; CLU_049049_1_1_3; -.
DR   OrthoDB; 9813395at2; -.
DR   UniPathway; UPA00342; -.
DR   Proteomes; UP000010471; 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: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   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   NCBIfam; TIGR00274; N-acetylmuramic acid 6-phosphate etherase; 1.
DR   PANTHER; PTHR10088; GLUCOKINASE REGULATORY PROTEIN; 1.
DR   PANTHER; PTHR10088:SF4; GLUCOKINASE REGULATORY PROTEIN; 1.
DR   Pfam; PF20741; GKRP-like_C; 1.
DR   Pfam; PF01380; SIS; 1.
DR   SUPFAM; SSF53697; SIS domain; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010471}.
FT   DOMAIN          59..222
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   ACT_SITE        87
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00068"
FT   ACT_SITE        118
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00068"
SQ   SEQUENCE   310 AA;  33237 MW;  D92285A5A1E30446 CRC64;
     MKNLEERGHL LTEQINPASQ KLDQLTSLEL VDLFNREDAK TLSAIAAARI ELAQAIDRTA
     LALSRGGRLF YVGAGTSGRL GVLDAAECPP TFCTPPELVQ GIIAGGAGAL VRSSEDLEDK
     PEDGAEAIAH RHVTELDVVV GITAGGTTPF VHGALQAARQ RGATTILIAC VPSEQVSTEA
     DLDIRLLVGP EVLAGSTRLK AGTVTKMALN ILSTSVMVRR GKVYGNRMVD VAVTNKKLHD
     RALRILQDLT SLSREEAGYL LELSGRQVKL ALVMHWTGLG KEEGDRLLAQ HQGDLRSAVQ
     SWNHNTMENS
//
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