ID K9TT19_9CYAN Unreviewed; 307 AA.
AC K9TT19;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=Oscil6304_5689 {ECO:0000313|EMBL:AFY85164.1};
OS Oscillatoria acuminata PCC 6304.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX NCBI_TaxID=56110 {ECO:0000313|EMBL:AFY85164.1, ECO:0000313|Proteomes:UP000010367};
RN [1] {ECO:0000313|EMBL:AFY85164.1, ECO:0000313|Proteomes:UP000010367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6304 {ECO:0000313|EMBL:AFY85164.1,
RC ECO:0000313|Proteomes:UP000010367};
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., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Oscillatoria acuminata PCC 6304.";
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; CP003607; AFY85164.1; -; Genomic_DNA.
DR RefSeq; WP_015151771.1; NC_019693.1.
DR AlphaFoldDB; K9TT19; -.
DR STRING; 56110.Oscil6304_5689; -.
DR KEGG; oac:Oscil6304_5689; -.
DR PATRIC; fig|56110.3.peg.6984; -.
DR eggNOG; COG2103; Bacteria.
DR HOGENOM; CLU_049049_1_1_3; -.
DR InParanoid; K9TT19; -.
DR OrthoDB; 9813395at2; -.
DR UniPathway; UPA00342; -.
DR Proteomes; UP000010367; 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; PF13580; SIS_2; 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:UP000010367}.
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 307 AA; 32901 MW; 8528505441BE41DD CRC64;
MTNLEERGHL LTEQVNPSSA NLDRLSSLEL VDLFNQEDAK TLAAIASART QLAQAIDLAA
DKLRQGGRLF YIGAGTSGRL GVLDAAECPP TFCTPPEMVQ GVIAGGAGAL IRSSEDLEDR
AEDGEDAVVR RHLTDLDVIV GITAGGTTPF VQGALQAARR RGTSTVFIAC VPAEQVEVPV
DIDIRLLVGP EILAGSTRLK AGTVTKMALN ILSTGVMVKL GKVYGNRMVD VSVTNKKLQD
RALRILEDLT GLSRQDAGFL LEKSGRSVKL ALIMYWTHLN KEEAQQLLET HNGQLRLAVD
SLKNPAP
//
