ID G4A9F9_AGGAC Unreviewed; 376 AA.
AC G4A9F9;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Anhydro-N-acetylmuramic acid kinase {ECO:0000256|HAMAP-Rule:MF_01270};
DE EC=2.7.1.170 {ECO:0000256|HAMAP-Rule:MF_01270};
DE AltName: Full=AnhMurNAc kinase {ECO:0000256|HAMAP-Rule:MF_01270};
GN Name=anmK {ECO:0000256|HAMAP-Rule:MF_01270};
GN ORFNames=SC1083_1473 {ECO:0000313|EMBL:EGY33357.1};
OS Aggregatibacter actinomycetemcomitans serotype e str. SC1083.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=907488 {ECO:0000313|EMBL:EGY33357.1, ECO:0000313|Proteomes:UP000005508};
RN [1] {ECO:0000313|EMBL:EGY33357.1, ECO:0000313|Proteomes:UP000005508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC1083 {ECO:0000313|EMBL:EGY33357.1,
RC ECO:0000313|Proteomes:UP000005508};
RA Chen C., Kittichotirat W., Asikainen S., Bumgarner R.;
RL Submitted (OCT-2010) 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 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:0000256|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:0000256|HAMAP-Rule:MF_01270};
CC -!- PATHWAY: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate
CC degradation. {ECO:0000256|HAMAP-Rule:MF_01270}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000256|HAMAP-Rule:MF_01270}.
CC -!- SIMILARITY: Belongs to the anhydro-N-acetylmuramic acid kinase family.
CC {ECO:0000256|HAMAP-Rule:MF_01270}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGY33357.1}.
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DR EMBL; AEJM01000029; EGY33357.1; -; Genomic_DNA.
DR RefSeq; WP_005558168.1; NZ_AEJM01000029.1.
DR AlphaFoldDB; G4A9F9; -.
DR SMR; G4A9F9; -.
DR PATRIC; fig|907488.3.peg.1440; -.
DR UniPathway; UPA00343; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000005508; Unassembled WGS sequence.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_01270; AnhMurNAc_kinase; 1.
DR InterPro; IPR005338; Anhydro_N_Ac-Mur_kinase.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR30605; ANHYDRO-N-ACETYLMURAMIC ACID KINASE; 1.
DR PANTHER; PTHR30605:SF0; ANHYDRO-N-ACETYLMURAMIC ACID KINASE; 1.
DR Pfam; PF03702; AnmK; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01270};
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01270};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_01270, ECO:0000313|EMBL:EGY33357.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01270};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01270}.
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01270"
SQ SEQUENCE 376 AA; 41385 MW; 4D8CE0DDE5E9DAAE CRC64;
MQQEYYLGIM SGTSLDGVDV ALMAFTEQPQ FIAGQFTSMP THLRQDLLQL VSHGTTTLQQ
LGELDQRLAL LYADAVNRFL TTHNLPSQHI RAIGCHGQTV WHAPQGDFPF TLQIGDMHLL
AARTDIDVVG DFRRKDMAFG GQGAPLVPAF HQALFYDERW ATVVLNIGGI SNISVLLPHQ
PIIGYDTGTG NALMDGWIER HLGKSYDADG QWARSGKVRL ELLAEMLKEP YFQLPPPKST
GRELFNLAWL EKTLAKTTAL LGEIPPQDVQ ATLLEFTAQS IALALNRLET ELPRRLLVCG
GGAKNGLLME RLQALLPNWQ YLPTNDAGLD VDYVEAAAFA WLAYRRINNL PSNLPSVTGA
KSAVSLGAIF PAEKIS
//
