ID W9UZP6_9GAMM Unreviewed; 367 AA.
AC W9UZP6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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:EXJ09312.1};
GN ORFNames=D791_03794 {ECO:0000313|EMBL:EXJ09312.1};
OS Nitrincola nitratireducens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Nitrincola.
OX NCBI_TaxID=1229521 {ECO:0000313|EMBL:EXJ09312.1, ECO:0000313|Proteomes:UP000019464};
RN [1] {ECO:0000313|Proteomes:UP000019464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK23 {ECO:0000313|Proteomes:UP000019464};
RA Singh A., Pinnaka A.K., Vaidya B.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXJ09312.1, ECO:0000313|Proteomes:UP000019464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK23 {ECO:0000313|EMBL:EXJ09312.1,
RC ECO:0000313|Proteomes:UP000019464};
RX PubMed=26481633; DOI=10.1016/j.syapm.2015.09.002;
RA Singh A., Vaidya B., Tanuku N.R., Pinnaka A.K.;
RT "Nitrincola nitratireducens sp. nov. isolated from a haloalkaline crater
RT lake.";
RL Syst. Appl. Microbiol. 38:555-562(2015).
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:EXJ09312.1}.
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DR EMBL; AONB01000027; EXJ09312.1; -; Genomic_DNA.
DR RefSeq; WP_036514300.1; NZ_AONB01000027.1.
DR AlphaFoldDB; W9UZP6; -.
DR STRING; 1229521.D791_03794; -.
DR PATRIC; fig|1229521.3.peg.3822; -.
DR OrthoDB; 9763949at2; -.
DR UniPathway; UPA00343; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000019464; 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:EXJ09312.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01270};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01270, ECO:0000313|EMBL:EXJ09312.1}.
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01270"
SQ SEQUENCE 367 AA; 40553 MW; C26CC33D4315F937 CRC64;
MSHYFIGIMS GTSLDSIDSV LVSFDTTFKL HGTYREAIPS DLKEKILRLT QPGQSEIEAL
AHLDPLLGEI FASNARALLE KYAVAEKDII AIGCHGQTLR HYPEQGFSLQ AGDPNIICER
TGILTIADFR RRDLASGGQG APLVPAFHDH LFRSDQQNRI IVNIGGMANL TFLPADPSAQ
VLGYDSGPGN VLLDAWIHQH KQRHFDEHGD WANSGHIHTE LLQTLQSHDY FKLTPPKSTG
REAFHLDWLE NVISTIATPI LPEDVQATLT ELTASSICDE IKRLEKDDKA DIFLCGGGAH
NAFLKSRIEQ HLGRPTLKTD SLGLDADWVE ACAFAWLAWR TLHHKTGNLP DVTGAKGKRI
LGGIYYP
//
