(data stored in SCRATCH zone)

SWISSPROT: A4F6M7_SACEN

ID   A4F6M7_SACEN            Unreviewed;       305 AA.
AC   A4F6M7;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   11-DEC-2019, entry version 90.
DE   RecName: Full=N-acetylmuramic acid 6-phosphate etherase {ECO:0000256|HAMAP-Rule:MF_00068, ECO:0000256|SAAS:SAAS00767172};
DE            Short=MurNAc-6-P etherase {ECO:0000256|HAMAP-Rule:MF_00068};
DE            EC=4.2.1.126 {ECO:0000256|HAMAP-Rule:MF_00068, ECO:0000256|SAAS:SAAS00767172};
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   OrderedLocusNames=SACE_0352 {ECO:0000313|EMBL:CAL99701.1};
GN   ORFNames=A8924_0747 {ECO:0000313|EMBL:PFG93504.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99701.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99701.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99701.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93504.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93504.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) 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       ECO:0000256|SAAS:SAAS00767196}.
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, ECO:0000256|SAAS:SAAS01114880};
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylmuramate degradation.
CC       {ECO:0000256|HAMAP-Rule:MF_00068, ECO:0000256|SAAS:SAAS00767189}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00068,
CC       ECO:0000256|SAAS:SAAS00767192}.
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,
CC       ECO:0000256|SAAS:SAAS00767176}.
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DR   EMBL; AM420293; CAL99701.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93504.1; -; Genomic_DNA.
DR   RefSeq; WP_009946499.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0352; -.
DR   EnsemblBacteria; CAL99701; CAL99701; SACE_0352.
DR   KEGG; sen:SACE_0352; -.
DR   eggNOG; ENOG4105E15; Bacteria.
DR   eggNOG; COG2103; LUCA.
DR   HOGENOM; HOG000084045; -.
DR   KO; K07106; -.
DR   OMA; CPPTFCT; -.
DR   OrthoDB; 1100044at2; -.
DR   BioCyc; SERY405948:SACE_RS01725-MONOMER; -.
DR   UniPathway; UPA00342; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
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: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.
DR   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR10088; PTHR10088; 1.
DR   PANTHER; PTHR10088:SF5; PTHR10088:SF5; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   TIGRFAMs; TIGR00274; TIGR00274; 1.
DR   PROSITE; PS01272; GCKR; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4F6M7.
DR   SWISS-2DPAGE; A4F6M7.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00068,
KW   ECO:0000256|SAAS:SAAS01098713};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00068, ECO:0000256|SAAS:SAAS00767171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   DOMAIN          61..223
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        89
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00068"
FT   ACT_SITE        120
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00068"
SQ   SEQUENCE   305 AA;  31533 MW;  C6D7DD1F1B0E9371 CRC64;
     MRDTERAVRV ESPTERSNPR TKDIDLLPTL DILHLLNSED RTVPAAVGRA LPELARAVDM
     AVSALRGGGR VHYVGAGTSG RLAVLDAAEL IPTFNVPPNW FVAHQAGGAG AFQRAVENAE
     DNADAGAATI EAEATGADFV LGLAASGRTP FVMGALDAAR RMGAGTGLVS ANPESAASSP
     AEVVIAVDTG PEPITGSTRM KAGTAQKLVL TSFSTSVMIR LGRTYSNLMV SMLATNAKLR
     GRTISILREA TNAPEADCEA ALTAADGDLK TALVHLLTGV DVERASAALA VSDGHVREAM
     RSLNA
//

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