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Database: UniProt
Entry: D9IQJ3_9GAMM
LinkDB: D9IQJ3_9GAMM
Original site: D9IQJ3_9GAMM 
ID   D9IQJ3_9GAMM            Unreviewed;       381 AA.
AC   D9IQJ3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   03-MAY-2023, 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:ADJ68311.1};
OS   Francisella noatunensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=657445 {ECO:0000313|EMBL:ADJ68311.1};
RN   [1] {ECO:0000313|EMBL:ADJ68311.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=3 {ECO:0000313|EMBL:ADJ68311.1};
RA   Calcutt M.J., Mutangadura T., Reilly T.J., Vojtech L., Hansen J.D.;
RT   "Pathogenicity islands and type VI secretion system genes from Francisella
RT   noatunensis.";
RL   Submitted (MAY-2010) 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}.
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DR   EMBL; HM171375; ADJ68311.1; -; Genomic_DNA.
DR   RefSeq; WP_014714928.1; NC_023029.1.
DR   AlphaFoldDB; D9IQJ3; -.
DR   GeneID; 45433473; -.
DR   UniPathway; UPA00343; -.
DR   UniPathway; UPA00544; -.
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   Transferase {ECO:0000256|HAMAP-Rule:MF_01270}.
FT   BINDING         13..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01270"
SQ   SEQUENCE   381 AA;  42188 MW;  16612765261AB8F3 CRC64;
     MDEYKYCIGI MSGTSLDGID VALCKIRGYG LATDIKLVNF ETYPYSEGLL NDIKQSLDLT
     RSNAQLLCNL NFKLGIEYAN AVKKLVTVSN LELEDIAFIA SHGQTIYHQA KNEDGFIKSS
     LQLGDAATIA YECRTTVVSN FRAGDIAAGG DGAPLVPYVD YILYSDKNKS RALHNIGGIA
     NTTIIPKNPN INDIYAFDTG PGNMMINRAM EVLFNRDYDK DGEIAASSIV IVDMLQELLQ
     NPYLALKPPK STGRELFGIE YTDYILDKYK QSNPKDIVHT LTIFTAESII KAYRDFVFDK
     VKLDQIIFTG GGAYNKFLIK TIKKLVKTEV LTFEYIGHNS DAKEAIAFAV LGNETLNHSY
     NNLPSATGAK DRVILGQVNI Y
//
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