(data stored in ACNUC7421 zone)

SWISSPROT: C6WFA5_ACTMD

ID   C6WFA5_ACTMD            Unreviewed;       308 AA.
AC   C6WFA5;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   08-MAY-2019, entry version 64.
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   OrderedLocusNames=Amir_0268 {ECO:0000313|EMBL:ACU34237.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34237.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34237.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
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. {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
CC       aldehyde intermediate with (E)-stereochemistry, followed by the
CC       syn addition of water to give product. {ECO:0000256|HAMAP-
CC       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; CP001630; ACU34237.1; -; Genomic_DNA.
DR   RefSeq; WP_012782900.1; NC_013093.1.
DR   STRING; 446462.Amir_0268; -.
DR   EnsemblBacteria; ACU34237; ACU34237; Amir_0268.
DR   KEGG; ami:Amir_0268; -.
DR   eggNOG; ENOG4105E15; Bacteria.
DR   eggNOG; COG2103; LUCA.
DR   HOGENOM; HOG000084045; -.
DR   KO; K07106; -.
DR   OMA; CPPTFCT; -.
DR   OrthoDB; 1100044at2; -.
DR   BioCyc; AMIR446462:G1GEY-278-MONOMER; -.
DR   UniPathway; UPA00342; -.
DR   Proteomes; UP000002213; 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:0016301; F:kinase activity; IEA:UniProtKB-KW.
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   PANTHER; PTHR10088; PTHR10088; 1.
DR   PANTHER; PTHR10088:SF5; PTHR10088:SF5; 1.
DR   Pfam; PF13580; SIS_2; 1.
DR   PROSITE; PS01272; GCKR; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6WFA5.
DR   SWISS-2DPAGE; C6WFA5.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00068,
KW   ECO:0000256|SAAS:SAAS01098713};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Kinase {ECO:0000313|EMBL:ACU34237.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   Transferase {ECO:0000313|EMBL:ACU34237.1}.
FT   DOMAIN       61    222       SIS. {ECO:0000259|PROSITE:PS51464}.
FT   ACT_SITE     89     89       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00068}.
FT   ACT_SITE    120    120       {ECO:0000256|HAMAP-Rule:MF_00068}.
SQ   SEQUENCE   308 AA;  31638 MW;  D7AAEBD50F0CCF41 CRC64;
     MTARGDVVRV ESPTEARNPR TGEIDRMSTL DVLRMINSED RGVPDAVAAV LPELARAADL
     AVAALRGGGR VHYVGAGTSG RLATLDAAEL PPTFNTPPDW FVAHHAGGAE ALVRAVENAE
     DQAATGAERI RAHAEPGDLV LGVTASGRTP FVLGALAAAH ELGARTALVS NNPSAPPVPV
     DVLITVDTGP EAIAGSTRMK AGSSQKLVLT AFSTAVMVRM GRTYSNLMVS VRATNAKLRG
     RTVRILSEAT GLDERECTDA LTAAGDDLKV ALVHLLSGSP APDAAEALTA TGGHVRQALT
     RLSAGATG
//

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