NANK_PASMU
ID NANK_PASMU Reviewed; 297 AA.
AC Q9CKB3;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=N-acetylmannosamine kinase {ECO:0000255|HAMAP-Rule:MF_01234};
DE EC=2.7.1.60 {ECO:0000255|HAMAP-Rule:MF_01234};
DE AltName: Full=ManNAc kinase {ECO:0000255|HAMAP-Rule:MF_01234};
DE AltName: Full=N-acetyl-D-mannosamine kinase {ECO:0000255|HAMAP-Rule:MF_01234};
GN Name=nanK {ECO:0000255|HAMAP-Rule:MF_01234}; OrderedLocusNames=PM1712;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC -!- FUNCTION: Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc)
CC to ManNAc-6-P. {ECO:0000255|HAMAP-Rule:MF_01234}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-D-mannosamine + ATP = ADP + an N-acyl-D-mannosamine
CC 6-phosphate + H(+); Xref=Rhea:RHEA:23832, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16062, ChEBI:CHEBI:30616, ChEBI:CHEBI:57666,
CC ChEBI:CHEBI:456216; EC=2.7.1.60; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01234};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 2/5.
CC {ECO:0000255|HAMAP-Rule:MF_01234}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01234}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. NanK subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01234}.
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; AE004439; AAK03796.1; -; Genomic_DNA.
DR RefSeq; WP_010907298.1; NC_002663.1.
DR PDB; 6JDA; X-ray; 2.90 A; A=1-291.
DR PDB; 6JDO; X-ray; 2.00 A; A/B=1-293.
DR PDBsum; 6JDA; -.
DR PDBsum; 6JDO; -.
DR AlphaFoldDB; Q9CKB3; -.
DR SMR; Q9CKB3; -.
DR STRING; 747.DR93_649; -.
DR EnsemblBacteria; AAK03796; AAK03796; PM1712.
DR KEGG; pmu:PM1712; -.
DR PATRIC; fig|272843.6.peg.1733; -.
DR HOGENOM; CLU_036604_0_4_6; -.
DR OMA; APNIDWR; -.
DR UniPathway; UPA00629; UER00681.
DR Proteomes; UP000000809; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009384; F:N-acylmannosamine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006051; P:N-acetylmannosamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_01234; ManNAc_kinase; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR023945; ManNAc_kinase_bac.
DR InterPro; IPR000600; ROK.
DR PANTHER; PTHR18964; PTHR18964; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; Kinase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT CHAIN 1..297
FT /note="N-acetylmannosamine kinase"
FT /id="PRO_0000095700"
FT BINDING 5..12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT BINDING 132..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:6JDO"
FT STRAND 10..19
FT /evidence="ECO:0007829|PDB:6JDO"
FT STRAND 22..30
FT /evidence="ECO:0007829|PDB:6JDO"
FT HELIX 36..50
FT /evidence="ECO:0007829|PDB:6JDO"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:6JDO"
FT STRAND 56..67
FT /evidence="ECO:0007829|PDB:6JDO"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6JDO"
FT HELIX 76..82
FT /evidence="ECO:0007829|PDB:6JDO"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:6JDO"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:6JDO"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:6JDO"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:6JDO"
FT STRAND 123..139
FT /evidence="ECO:0007829|PDB:6JDO"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:6JDO"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:6JDO"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:6JDO"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:6JDO"
FT HELIX 180..187
FT /evidence="ECO:0007829|PDB:6JDO"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6JDO"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:6JDO"
FT HELIX 208..232
FT /evidence="ECO:0007829|PDB:6JDO"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:6JDO"
FT TURN 242..245
FT /evidence="ECO:0007829|PDB:6JDO"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:6JDO"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:6JDO"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:6JDO"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:6JDA"
FT HELIX 277..291
FT /evidence="ECO:0007829|PDB:6JDO"
SQ SEQUENCE 297 AA; 31351 MW; EE531E9EE06A4CF9 CRC64;
MRCLALDIGG TKIASAIVTD GKIEQRQQIA TPQADAANAM HDTLANILAL YAGQFDYVAV
ASTGIINHGV LTALNPKNLG GLAEFPLKES IARHTDKPIG LLNDVQAAAC AEYKDEDKNA
VQNFVFITVS TGVGGGIILE RRLLTEPNGV AGHIGHTLAD PNGPVCGCGR VGCVEAVAAG
RAIEAVSSQW NPPCTPKQAF ELFRKNDEKA TALIQRSASA IANLIADLVI GLDVQKVVVG
GSVGLAEGYL PLVKQYLNMM PHFYHCTVEQ ARHGQDAGLL GAAWWVADCL KQGVHLK
