ID I3CND0_9BURK Unreviewed; 372 AA.
AC I3CND0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=GWL_45630 {ECO:0000313|EMBL:EIJ45123.1};
OS Herbaspirillum sp. GW103.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1175306 {ECO:0000313|EMBL:EIJ45123.1, ECO:0000313|Proteomes:UP000004194};
RN [1] {ECO:0000313|EMBL:EIJ45123.1, ECO:0000313|Proteomes:UP000004194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW103 {ECO:0000313|EMBL:EIJ45123.1,
RC ECO:0000313|Proteomes:UP000004194};
RX PubMed=22815460; DOI=10.1128/JB.00806-12;
RA Lee G.W., Lee K.J., Chae J.C.;
RT "Genome sequence of Herbaspirillum sp. strain GW103, a plant growth-
RT promoting bacterium.";
RL J. Bacteriol. 194:4150-4150(2012).
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:EIJ45123.1}.
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DR EMBL; AJVC01000006; EIJ45123.1; -; Genomic_DNA.
DR RefSeq; WP_008334696.1; NZ_AJVC01000006.1.
DR AlphaFoldDB; I3CND0; -.
DR STRING; 1175306.GWL_45630; -.
DR PATRIC; fig|1175306.3.peg.4429; -.
DR eggNOG; COG2377; Bacteria.
DR OrthoDB; 9763949at2; -.
DR UniPathway; UPA00343; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000004194; 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:EIJ45123.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01270};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01270}.
FT BINDING 14..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01270"
SQ SEQUENCE 372 AA; 39058 MW; 5643AA504C730624 CRC64;
MNDSSQLYIG LMSGTSLDGV DGVLAAFDGQ AVSATLAAAY VPFPAHLRAD LMALQAAGPN
EIEREALAAN ALAVHYADCV AQLLLQAGKS AADVRMVGVH GQTIRHRPEL GFTRQSNNAA
LLAELCAIDV VADFRSRDVA AGGQGAPLVP AFHRALFGDA TQSRVVVNIG GIANISILPA
DEEGAYGFDT GPGNALMDGW IHLHQQRPYD ANGHWGASGQ VHAGLLAQLR DEDFFRAAPP
KSSGRDLFHL DWLQAALLRT GAALAPEDVQ ATLAMLTAST IAEAILAHAP AARQVYVCGG
GAENALLMRL LQQQLQDRAI VQSTAVLGVA PQHVEALAFA WLARRFDLRL PGNLPAVTGA
RGLRVLGALY PA
//
