(data stored in SCRATCH zone)

SWISSPROT: B4STG0_STRM5

ID   B4STG0_STRM5            Unreviewed;       378 AA.
AC   B4STG0;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=Anhydro-N-acetylmuramic acid kinase {ECO:0000256|HAMAP-Rule:MF_01270, ECO:0000256|SAAS:SAAS00951634};
DE            EC=2.7.1.170 {ECO:0000256|HAMAP-Rule:MF_01270, ECO:0000256|SAAS:SAAS00951631};
DE   AltName: Full=AnhMurNAc kinase {ECO:0000256|HAMAP-Rule:MF_01270};
GN   Name=anmK {ECO:0000256|HAMAP-Rule:MF_01270};
GN   OrderedLocusNames=Smal_0298 {ECO:0000313|EMBL:ACF50003.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50003.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF50003.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF50003.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the specific phosphorylation of 1,6-anhydro-N-
CC       acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of
CC       the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the
CC       utilization of anhMurNAc either imported from the medium or
CC       derived from its own cell wall murein, and thus plays a role in
CC       cell wall recycling. {ECO:0000256|HAMAP-Rule:MF_01270,
CC       ECO:0000256|SAAS:SAAS00951629}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP +
CC         H(+) + 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:0000256|HAMAP-Rule:MF_01270,
CC         ECO:0000256|SAAS:SAAS01124448};
CC   -!- PATHWAY: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate
CC       degradation. {ECO:0000256|HAMAP-Rule:MF_01270,
CC       ECO:0000256|SAAS:SAAS00951630}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC       {ECO:0000256|HAMAP-Rule:MF_01270, ECO:0000256|SAAS:SAAS00951625}.
CC   -!- SIMILARITY: Belongs to the anhydro-N-acetylmuramic acid kinase
CC       family. {ECO:0000256|HAMAP-Rule:MF_01270,
CC       ECO:0000256|SAAS:SAAS00951641}.
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DR   EMBL; CP001111; ACF50003.1; -; Genomic_DNA.
DR   STRING; 391008.Smal_0298; -.
DR   EnsemblBacteria; ACF50003; ACF50003; Smal_0298.
DR   KEGG; smt:Smal_0298; -.
DR   eggNOG; ENOG4105ED7; Bacteria.
DR   eggNOG; COG2377; LUCA.
DR   HOGENOM; HOG000256309; -.
DR   KO; K09001; -.
DR   OMA; HGQTVYH; -.
DR   UniPathway; UPA00343; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000001867; Chromosome.
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; B4STG0.
DR   SWISS-2DPAGE; B4STG0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01270,
KW   ECO:0000256|SAAS:SAAS00951636};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01270,
KW   ECO:0000256|SAAS:SAAS00951635};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01270,
KW   ECO:0000256|SAAS:SAAS00951633};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01270,
KW   ECO:0000256|SAAS:SAAS00951627};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01270,
KW   ECO:0000256|SAAS:SAAS00951632}.
FT   NP_BIND      21     28       ATP. {ECO:0000256|HAMAP-Rule:MF_01270}.
SQ   SEQUENCE   378 AA;  39774 MW;  A36A84F56B83C61D CRC64;
     MPAMNTTADS DAPLYLGLMS GTSADGIDAA LVQFPASGGC RFVHGLTARW EPVLRARLVA
     LGEGGPLDSL EELGELDARI AIRFAEAANQ LLAEAGVDRS QVRAIGSHGQ TVRHRPLADP
     AFTVQLGDGN RIAELTGITT VCDFRRRDVA AGGHGAPLMP AFHLGMLGTA DEDRAVLNLG
     GIANLTLIPR EGAVRGFDTG PANALMDAWC QRHTGRTFDA DGAYAASGAV DEGLLAGWRS
     DPWFALPPPK STGREQFHLA WAEAHMGEGQ YAAADIQATL LELTVATVVD ALLAQQPRTR
     RLLVCGGGMR NTQLMRRLAA QLPGVVVESS AVHGLDPEYV EAMGFAWLAQ RTMDGLAGNL
     PSVTGAKGPR ILGAIHLA
//

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