(data stored in SCRATCH3701 zone)

SWISSPROT: ANMK_VIBVY

ID   ANMK_VIBVY              Reviewed;         370 AA.
AC   Q7MNL7;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   11-DEC-2019, entry version 89.
DE   RecName: Full=Anhydro-N-acetylmuramic acid kinase {ECO:0000255|HAMAP-Rule:MF_01270};
DE            EC=2.7.1.170 {ECO:0000255|HAMAP-Rule:MF_01270};
DE   AltName: Full=AnhMurNAc kinase {ECO:0000255|HAMAP-Rule:MF_01270};
GN   Name=anmK {ECO:0000255|HAMAP-Rule:MF_01270}; OrderedLocusNames=VV0699;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
CC   -!- FUNCTION: Catalyzes the specific phosphorylation of 1,6-anhydro-N-
CC       acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the
CC       1,6-anhydro ring, generating MurNAc-6-P. Is required for the
CC       utilization of anhMurNAc either imported from the medium or derived
CC       from its own cell wall murein, and thus plays a role in cell wall
CC       recycling. {ECO:0000255|HAMAP-Rule:MF_01270}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) +
CC         N-acetyl-D-muramate 6-phosphate; Xref=Rhea:RHEA:24952,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58690, ChEBI:CHEBI:58722, ChEBI:CHEBI:456216;
CC         EC=2.7.1.170; Evidence={ECO:0000255|HAMAP-Rule:MF_01270};
CC   -!- PATHWAY: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate
CC       degradation. {ECO:0000255|HAMAP-Rule:MF_01270}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC       {ECO:0000255|HAMAP-Rule:MF_01270}.
CC   -!- SIMILARITY: Belongs to the anhydro-N-acetylmuramic acid kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01270}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC93462.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; BA000037; BAC93462.1; ALT_INIT; Genomic_DNA.
DR   SMR; Q7MNL7; -.
DR   STRING; 672.VV93_v1c06360; -.
DR   EnsemblBacteria; BAC93462; BAC93462; BAC93462.
DR   KEGG; vvy:VV0699; -.
DR   PATRIC; fig|196600.6.peg.717; -.
DR   HOGENOM; HOG000256309; -.
DR   KO; K09001; -.
DR   OMA; QTIRHEP; -.
DR   UniPathway; UPA00343; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000002675; Chromosome I.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0097175; P:1,6-anhydro-N-acetyl-beta-muramic acid catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006040; P:amino sugar metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01270; AnhMurNAc_kinase; 1.
DR   InterPro; IPR005338; Anhydro_N_Ac-Mur_kinase.
DR   PANTHER; PTHR30605; PTHR30605; 1.
DR   Pfam; PF03702; AnmK; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7MNL7.
DR   SWISS-2DPAGE; Q7MNL7.
KW   ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..370
FT                   /note="Anhydro-N-acetylmuramic acid kinase"
FT                   /id="PRO_0000250082"
FT   NP_BIND         13..20
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01270"
SQ   SEQUENCE   370 AA;  40766 MW;  0D35B740F6E01946 CRC64;
     MSTKELYIGV MSGTSMDGVD CALVEFDQEQ VRLIAHSDYP MPADLRQQLL SVCTGQATNL
     KQIGELDHRL GHLFADAVMD LLSQAGVDAS QICAIGNHGQ TVFHQPNGEF PFTTQLGDAN
     IIATRTNIDT VADFRRKDMA LGGQGAPLVP AFHQSVFALQ DSTTVVLNIG GIANISVLHP
     TRPVLGYDTG PGNMLMDAWC ETHTQQNYDK DARFALQGEV NEALLNSLLQ EPYLHQDAPK
     STGRELFNME WLTAKLQGQN YRSEDVQRTL CEYTALTISK EVERFRYGPT PQLLVCGGGA
     RNPLLMQRLQ QQLSHWQVST TDAKGVSGDY MEAMAFAWLA YRHMHRLPSN LPEVTGASRL
     ASLGVLYPKA
//

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