ID B9L4J5_THERP Unreviewed; 417 AA.
AC B9L4J5;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
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:ACM06884.1};
GN OrderedLocusNames=trd_A0709 {ECO:0000313|EMBL:ACM06884.1};
OS Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OG Plasmid Tros {ECO:0000313|Proteomes:UP000000447}.
OC Bacteria; Thermomicrobiota; Thermomicrobia; Thermomicrobiales;
OC Thermomicrobiaceae; Thermomicrobium.
OX NCBI_TaxID=309801 {ECO:0000313|EMBL:ACM06884.1, ECO:0000313|Proteomes:UP000000447};
RN [1] {ECO:0000313|EMBL:ACM06884.1, ECO:0000313|Proteomes:UP000000447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27502 / DSM 5159 / P-2
RC {ECO:0000313|Proteomes:UP000000447};
RC PLASMID=Tros {ECO:0000313|Proteomes:UP000000447};
RX PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA Eisen J.A.;
RT "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT Thermomicrobium roseum.";
RL PLoS ONE 4:E4207-E4207(2009).
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}.
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DR EMBL; CP001276; ACM06884.1; -; Genomic_DNA.
DR RefSeq; WP_012642871.1; NC_011961.1.
DR AlphaFoldDB; B9L4J5; -.
DR KEGG; tro:trd_A0709; -.
DR eggNOG; COG2377; Bacteria.
DR HOGENOM; CLU_038782_1_0_0; -.
DR OrthoDB; 9763949at2; -.
DR UniPathway; UPA00343; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000000447; Plasmid Tros.
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:ACM06884.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01270};
KW Plasmid {ECO:0000313|EMBL:ACM06884.1};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01270, ECO:0000313|EMBL:ACM06884.1}.
FT REGION 397..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 17..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01270"
SQ SEQUENCE 417 AA; 44602 MW; 2F42FF24412644EE CRC64;
MRTALSGNRL CIGLLSGTSA DAIDAALVRI RGAGPEAQLH LLAYRARPFP PLVRRELFQL
FEQAPPALER LCTLHVILGE LFAEAAMTLC RAAGCSLDEV FVIGSHGQTV WHQPAPSSLL
TLAARGTLQI GDPAVIAERT GVPVVADFRA ADMAAGGQGA PLTPYLDWVV LRHPTRHRAI
QNIGGIGNVT YLPASAPRED VFAFDTGPGN MVIDGVVQLL TTGELDCDRN GALAAQGRVD
RVLLERLLAD PFLDQPPPKT TGRERYGLPF ARQLLNEFGL PAGILRDPRV PATLRQRACD
LVATVTAFTA HAIAESYRRW LPPIDEVVVS GGGARNPSLM RVLRDLLAPV PVVPVEALGL
DSAAKEAMLF ALLAHDACFG LPTNVPSATG ARRAVTLGSL TPPNGWKERA NREEEQP
//
