Reviewed, UniProtKB/Swiss-Prot P77570 (ANMK_ECOLI)

Names and origin

Protein names

Recommended name:
    Anhydro-N-acetylmuramic acid kinase
    EC=2.7.1.n1
Alternative name(s):
    AnhMurNAc kinase

Gene names

Name:	anmK
Synonyms:	ydhH
Ordered Locus Names:	b1640, JW1632

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. Ref.4 Ref.5
Catalytic activity	ATP + 1,6-anhydro-N-acetylmuramic acid + H2O = ADP + N-acetylmuramic acid 6-phosphate. Ref.4
Enzyme regulation	Strongly inhibited by ADP. Ref.4
Pathway	Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. HAMAP MF_01270 Cell wall biogenesis; peptidoglycan recycling. HAMAP MF_01270
Sequence similarities	Belongs to the anhydro-N-acetylmuramic acid kinase family.
Biophysicochemical properties	Kinetic parameters: KM=1 mM for anhMurNAc HAMAP MF_01270 KM=1 mM for ATP Vmax=180 µmol/min/mg enzyme pH dependence: Optimum pH is 10-11. Inactive at pH 4.5.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	amino sugar metabolic process Inferred from electronic annotation. Source: HAMAP peptidoglycan turnover Inferred from electronic annotation. Source: HAMAP
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP kinase activity Inferred from electronic annotation. Source: UniProtKB-KW phosphotransferase activity, alcohol group as acceptor Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 369	369	Anhydro-N-acetylmuramic acid kinase HAMAP MF_01270		PRO_0000214821
Regions
	Nucleotide binding	12 – 19	8	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	P77570-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: E0B439314E60F51B	FASTA	369	39,496
	10 20 30 40 50 60 MKSGRFIGVM SGTSLDGVDV VLATIDEHRV AQLASLSWPI PVSLKQAVLD ICQGQQLTLS 70 80 90 100 110 120 QFGQLDTQLG QLFADAVNAL LKEQNLQARD IVAIGCHGQT VWHEPTGVAP HTLQIGDNNQ 130 140 150 160 170 180 IVARTGITVV GDFRRRDIAL GGQGAPLVPA FHHALLAHPT ERRMVLNIGG IANLSLLIPG 190 200 210 220 230 240 QPVGGYDTGP GNMLMDAWIW RQAGKPYDKD AEWARAGKVI LPLLQNMLSD PYFSQPAPKS 250 260 270 280 290 300 TGREYFNYGW LERHLRHFPG VDPRDVQATL AELTAVTISE QVLLSGGCER LMVCGGGSRN 310 320 330 340 350 360 PLLMARLAAL LPGTEVTTTD AVGISGDDME ALAFAWLAWR TLAGLPGNLP SVTGASQETV LGAIFPANP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate." Uehara T., Suefuji K., Valbuena N., Meehan B., Donegan M., Park J.T. J. Bacteriol. 187:3643-3649(2005) [PubMed: 15901686] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: K12 / MG1655 / ATCC 47076.
[5]	"MurQ etherase is required by Escherichia coli in order to metabolize anhydro-N-acetylmuramic acid obtained either from the environment or from its own cell wall." Uehara T., Suefuji K., Jaeger T., Mayer C., Park J.T. J. Bacteriol. 188:1660-1662(2006) [PubMed: 16452451] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U00096 Genomic DNA. Translation: AAC74712.1. AP009048 Genomic DNA. Translation: BAA15401.1.
PIR	B64921.
RefSeq	AP_002262.1. NP_416157.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:11731N.
STRING	P77570.
Genome annotation databases
GeneID	946810.
GenomeReviews	Gene locus JW1632 in contig AP009048_GR. Gene locus b1640 in contig U00096_GR.
KEGG	ecj:JW1632. eco:b1640.
Organism-specific databases
EchoBASE	EB3700.
EcoGene	EG13942. anmK.
CMR	Search...
Phylogenomic databases
HOGENOM	P77570.
OMA	GSHGQTV.
Enzyme and pathway databases
BioCyc	EcoCyc:G6880-MON. MetaCyc:G6880-MON.
Gene expression databases
Genevestigator	P77570.
Family and domain databases
HAMAP	MF_01270. [Tree]
InterPro	IPR005338. Anhydro_N_Ac-Mur_kinase. [Graphical view]
Pfam	PF03702. UPF0075. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ANMK_ECOLI

Accession

Primary (citable) accession number: P77570

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	February 1, 1997
Last modified:	November 3, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)