ID S9SGZ7_PAEAL Unreviewed; 396 AA.
AC S9SGZ7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
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 ECO:0000313|EMBL:EPY05082.1};
GN ORFNames=PAALTS15_21948 {ECO:0000313|EMBL:EPY05082.1};
OS Paenibacillus alvei TS-15.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1117108 {ECO:0000313|EMBL:EPY05082.1, ECO:0000313|Proteomes:UP000015344};
RN [1] {ECO:0000313|EMBL:EPY05082.1, ECO:0000313|Proteomes:UP000015344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TS-15 {ECO:0000313|EMBL:EPY05082.1,
RC ECO:0000313|Proteomes:UP000015344};
RA Strain E.A., Brown E., Allard M.W., Luo Y.L.;
RL Submitted (MAY-2013) 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:EPY05082.1}.
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DR EMBL; ATMT01000071; EPY05082.1; -; Genomic_DNA.
DR AlphaFoldDB; S9SGZ7; -.
DR PATRIC; fig|1117108.3.peg.4524; -.
DR eggNOG; COG2377; Bacteria.
DR UniPathway; UPA00343; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000015344; 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:EPY05082.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01270};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01270}.
FT BINDING 20..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01270"
SQ SEQUENCE 396 AA; 42631 MW; 3EC976BB57BA3C68 CRC64;
MRTRSLAVKS EHIIIGLMSG TSLDGIDAAV VRIQGAGVES RADMIAFHCK EYDEELRERL
KRLCTRGGTS TEEICMMNAY MGEMLAQAAC EAASNAGISM KDVDFVSSHG QTIWHQPIVD
KADRCAVPST LQIGDISIIA KHTGVPVIGD YRPADMAVGG QGAPLTPYAD YLLLRDSEAG
RIAQNIGGIG NCTILPAGGD QSKVTAFDTG PGNMLIDQAI YQLSGGAYGY DRNGEWASRG
QVNTELLDDL LAHPYYAEPP VKTTGREMFG TDYALQWIEH GRMLGLSAED IVATFTALTA
RTIADAYRQF VFPQHRIRDV IVSGGGARNA TLMRWLAEEL PEQNVTASDE MGLPGDAKEA
IAFALLANDF IHGVPNNLPR VTGAVRPTIM GKLAMP
//
