ID S3JWP2_TREMA Unreviewed; 416 AA.
AC S3JWP2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, 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=HMPREF9194_00710 {ECO:0000313|EMBL:EPF30393.1};
OS Treponema maltophilum ATCC 51939.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=1125699 {ECO:0000313|EMBL:EPF30393.1, ECO:0000313|Proteomes:UP000014541};
RN [1] {ECO:0000313|EMBL:EPF30393.1, ECO:0000313|Proteomes:UP000014541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51939 {ECO:0000313|EMBL:EPF30393.1,
RC ECO:0000313|Proteomes:UP000014541};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Leonetti C., Blanton J.M.,
RA Dewhirst F.E., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Treponema maltophilum ATCC 51939.";
RL Submitted (APR-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:EPF30393.1}.
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DR EMBL; ATFF01000006; EPF30393.1; -; Genomic_DNA.
DR RefSeq; WP_016525004.1; NZ_KE332518.1.
DR AlphaFoldDB; S3JWP2; -.
DR STRING; 1125699.HMPREF9194_00710; -.
DR PATRIC; fig|1125699.3.peg.723; -.
DR eggNOG; COG2377; Bacteria.
DR HOGENOM; CLU_038782_1_0_12; -.
DR OrthoDB; 9763949at2; -.
DR UniPathway; UPA00343; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000014541; 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};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01270};
KW Reference proteome {ECO:0000313|Proteomes:UP000014541};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01270}.
FT BINDING 21..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01270"
SQ SEQUENCE 416 AA; 45038 MW; E4D366CAB3910D82 CRC64;
MDRLGRIRQK TTKTAVGLMS GTSVDGIDAV LLDISRTPPK AENRRKNAGL FGASDKLPEL
PELTVKERAF VTLDYPEDVR QKLLALASGN TGGSEELCVL NFYLGELFAD ACFEVCKKAG
VSIGSVDFIG SHGHTVFHAP QERLVFGKRI KSTLQIGEGA VIAERTGCIT VSDFRVRDTA
AGGFGAPLVP FSEYLLYRER GKVIALQNIG GIGNITILPA DENINGIIAF DTGPGNMIID
GLVRILTGGK QNYDKDGAIA LRGKVDEELL GFLKKDPYLY EAPPKTTGRE HYTADFIQAF
YRKGKELNLA PETIVRTASY YTAFCIARSL TDFKLPQPQK LIVGGGGSKN PVILAHLREL
LPHCAVMTNE DIGKNGDSKE ACAFAVLAHE TLYERPNNVP SATGAHSFVV MGKISF
//
