ID   A0A2S8SRP0_9BACT        Unreviewed;       366 AA.
AC   A0A2S8SRP0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   17-JUN-2020, entry version 8.
DE   RecName: Full=Anhydro-N-acetylmuramic acid kinase {ECO:0000256|HAMAP-Rule:MF_01270, ECO:0000256|SAAS:SAAS01259226};
DE            EC=2.7.1.170 {ECO:0000256|HAMAP-Rule:MF_01270, ECO:0000256|SAAS:SAAS01259222};
DE   AltName: Full=AnhMurNAc kinase {ECO:0000256|HAMAP-Rule:MF_01270};
GN   Name=anmK {ECO:0000256|HAMAP-Rule:MF_01270};
GN   ORFNames=B1R32_11135 {ECO:0000313|EMBL:PQV63474.1};
OS   Abditibacterium utsteinense.
OC   Bacteria; Abditibacteriota; Abditibacteria; Abditibacteriales;
OC   Abitibacteriaceae; Abditibacterium.
OX   NCBI_TaxID=1960156 {ECO:0000313|EMBL:PQV63474.1, ECO:0000313|Proteomes:UP000237684};
RN   [1] {ECO:0000313|EMBL:PQV63474.1, ECO:0000313|Proteomes:UP000237684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29911 {ECO:0000313|EMBL:PQV63474.1,
RC   ECO:0000313|Proteomes:UP000237684};
RX   PubMed=29475572;
RA   Tahon G., Tytgat B., Lebbe L., Carlier A., Willems A.;
RT   "Abditibacterium utsteinense sp. nov., the first cultivated member of
RT   candidate phylum FBP, isolated from ice-free Antarctic soil samples.";
RL   Syst. Appl. Microbiol. 0:0-0(2018).
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       ECO:0000256|SAAS:SAAS01259221}.
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         ECO:0000256|SAAS:SAAS01259227};
CC   -!- PATHWAY: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate
CC       degradation. {ECO:0000256|HAMAP-Rule:MF_01270,
CC       ECO:0000256|SAAS:SAAS01259229}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC       {ECO:0000256|HAMAP-Rule:MF_01270, ECO:0000256|SAAS:SAAS01259230}.
CC   -!- SIMILARITY: Belongs to the anhydro-N-acetylmuramic acid kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01270, ECO:0000256|SAAS:SAAS01259232}.
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:PQV63474.1}.
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DR   EMBL; NIGF01000011; PQV63474.1; -; Genomic_DNA.
DR   UniPathway; UPA00343; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000237684; 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   HAMAP; MF_01270; AnhMurNAc_kinase; 1.
DR   InterPro; IPR005338; Anhydro_N_Ac-Mur_kinase.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR30605; PTHR30605; 1.
DR   Pfam; PF03702; AnmK; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01270,
KW   ECO:0000256|SAAS:SAAS01259224};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01270,
KW   ECO:0000256|SAAS:SAAS01259225};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01270, ECO:0000256|SAAS:SAAS01259231,
KW   ECO:0000313|EMBL:PQV63474.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01270,
KW   ECO:0000256|SAAS:SAAS01259233};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237684};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01270,
KW   ECO:0000256|SAAS:SAAS01259223}.
FT   NP_BIND         9..16
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01270"
SQ   SEQUENCE   366 AA;  38847 MW;  EEF3DB2DDC65D7F2 CRC64;
     MKVIGLMSGT SCDGIDAALC EISGSGETLR AELLDFSCFA FEENLRERIL RACNNGCDAQ
     EVARLNVVLG EEFARAANNL IEKHGKVDLI GSHGQTVCHL PAEKVTLQIG EAAIIAARTG
     TDVVADFRPR DLAEGGQGAP LVPYVDWILL RHSTKNRVAL NIGGIANASI LPANCALKDV
     RAWDTGPGNM VIDACAEALF GVPFDKNGEL AARGNPASWF YGDMARLSSF FVESPPKSAG
     REEFGARFAA GFHALNRDLH DILAEVTWIS AHSIANSLRD FSGFGEDFEL IISGGGAFNS
     TLLQMLRDEI PGATILRSDE IGIRADAKEA IAFAILASET INGIPTNVPG ATGARKAAIL
     GKIVRA
//