ANMK_SHEON
ID ANMK_SHEON Reviewed; 369 AA.
AC Q8EHB5;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Anhydro-N-acetylmuramic acid kinase {ECO:0000255|HAMAP-Rule:MF_01270};
DE EC=2.7.1.170 {ECO:0000255|HAMAP-Rule:MF_01270};
DE AltName: Full=AnhMurNAc kinase {ECO:0000255|HAMAP-Rule:MF_01270};
GN Name=anmK {ECO:0000255|HAMAP-Rule:MF_01270}; OrderedLocusNames=SO_1313;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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:0000255|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:0000255|HAMAP-Rule:MF_01270};
CC -!- PATHWAY: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate
CC degradation. {ECO:0000255|HAMAP-Rule:MF_01270}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000255|HAMAP-Rule:MF_01270}.
CC -!- SIMILARITY: Belongs to the anhydro-N-acetylmuramic acid kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_01270}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014299; AAN54378.1; -; Genomic_DNA.
DR RefSeq; NP_716933.1; NC_004347.2.
DR RefSeq; WP_011071524.1; NZ_CP053946.1.
DR PDB; 3CQY; X-ray; 2.30 A; A/B=1-369.
DR PDBsum; 3CQY; -.
DR AlphaFoldDB; Q8EHB5; -.
DR SMR; Q8EHB5; -.
DR STRING; 211586.SO_1313; -.
DR PaxDb; Q8EHB5; -.
DR KEGG; son:SO_1313; -.
DR PATRIC; fig|211586.12.peg.1264; -.
DR eggNOG; COG2377; Bacteria.
DR HOGENOM; CLU_038782_0_0_6; -.
DR OMA; GQTIRHE; -.
DR OrthoDB; 736294at2; -.
DR PhylomeDB; Q8EHB5; -.
DR BioCyc; SONE211586:G1GMP-1213-MON; -.
DR BRENDA; 2.7.1.170; 5706.
DR UniPathway; UPA00343; -.
DR UniPathway; UPA00544; -.
DR EvolutionaryTrace; Q8EHB5; -.
DR Proteomes; UP000008186; Chromosome.
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 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..369
FT /note="Anhydro-N-acetylmuramic acid kinase"
FT /id="PRO_0000250057"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01270"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:3CQY"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:3CQY"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:3CQY"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:3CQY"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:3CQY"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:3CQY"
FT HELIX 58..84
FT /evidence="ECO:0007829|PDB:3CQY"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:3CQY"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:3CQY"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:3CQY"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:3CQY"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:3CQY"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:3CQY"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3CQY"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:3CQY"
FT HELIX 148..156
FT /evidence="ECO:0007829|PDB:3CQY"
FT STRAND 163..177
FT /evidence="ECO:0007829|PDB:3CQY"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:3CQY"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:3CQY"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:3CQY"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:3CQY"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:3CQY"
FT HELIX 222..229
FT /evidence="ECO:0007829|PDB:3CQY"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:3CQY"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:3CQY"
FT HELIX 249..255
FT /evidence="ECO:0007829|PDB:3CQY"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:3CQY"
FT HELIX 264..286
FT /evidence="ECO:0007829|PDB:3CQY"
FT STRAND 288..296
FT /evidence="ECO:0007829|PDB:3CQY"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:3CQY"
FT HELIX 302..311
FT /evidence="ECO:0007829|PDB:3CQY"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:3CQY"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:3CQY"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:3CQY"
FT HELIX 330..343
FT /evidence="ECO:0007829|PDB:3CQY"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:3CQY"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:3CQY"
SQ SEQUENCE 369 AA; 39810 MW; 8C302953BC66DB8B CRC64;
MNKAYYIGLM SGTSMDGVDA VLVDFAGEQP QLIGTHTETI PTHLLKGLQR LCLPGTDEIN
RLGRLDRSVG KLFALAVNNL LAKTKIAKDE IIAIGSHGQT VRHMPNLEVG FTLQIGDPNT
IATETGIDVI ADFRRKDIAL GGQGAPLVPA FHQQTFAQVG KKRVILNIGG IANITYLPGN
SEEVLGFDTG PGNTLIDAWV QQVKNESYDK NGAWAASGKT DPQLLAQLLS HPYFSLAYPK
STGRELFNQA WLEQQLSAFN QLNEEDIQST LLDLTCHSIA QDILKLAQEG ELFVCGGGAF
NAELMQRLAA LLPGYRIDTT SALGVDPKWA EGIAFAWLAM RYQLGLPANL PAVTGASREA
ILGGRFSAK
