NANK_HAEI8
ID NANK_HAEI8 Reviewed; 300 AA.
AC Q4QP43;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=NTHI0230;
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP;
RX PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA Munson R.S. Jr.;
RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(2005).
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}.
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DR EMBL; CP000057; AAX87204.1; -; Genomic_DNA.
DR RefSeq; WP_011271901.1; NC_007146.2.
DR PDB; 6JDB; X-ray; 2.65 A; A=1-291.
DR PDB; 6JDC; X-ray; 2.27 A; A=1-290.
DR PDBsum; 6JDB; -.
DR PDBsum; 6JDC; -.
DR AlphaFoldDB; Q4QP43; -.
DR SMR; Q4QP43; -.
DR EnsemblBacteria; AAX87204; AAX87204; NTHI0230.
DR KEGG; hit:NTHI0230; -.
DR HOGENOM; CLU_036604_0_4_6; -.
DR OMA; APNIDWR; -.
DR OrthoDB; 1130699at2; -.
DR UniPathway; UPA00629; UER00681.
DR Proteomes; UP000002525; 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.
DR PROSITE; PS01125; ROK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; Kinase; Metal-binding;
KW Nucleotide-binding; Transferase; Zinc.
FT CHAIN 1..300
FT /note="N-acetylmannosamine kinase"
FT /id="PRO_0000301459"
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:6JDC"
FT STRAND 10..19
FT /evidence="ECO:0007829|PDB:6JDC"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:6JDC"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:6JDC"
FT HELIX 36..50
FT /evidence="ECO:0007829|PDB:6JDC"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:6JDC"
FT STRAND 56..67
FT /evidence="ECO:0007829|PDB:6JDC"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6JDC"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:6JDC"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6JDB"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:6JDC"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:6JDC"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:6JDC"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:6JDC"
FT STRAND 123..139
FT /evidence="ECO:0007829|PDB:6JDC"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:6JDB"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:6JDC"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:6JDC"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:6JDC"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6JDC"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:6JDC"
FT HELIX 180..184
FT /evidence="ECO:0007829|PDB:6JDC"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:6JDB"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:6JDB"
FT HELIX 211..232
FT /evidence="ECO:0007829|PDB:6JDC"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:6JDC"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:6JDC"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:6JDC"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:6JDC"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:6JDC"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:6JDC"
FT HELIX 277..288
FT /evidence="ECO:0007829|PDB:6JDC"
SQ SEQUENCE 300 AA; 31964 MW; ECDD3F41A7A8DED2 CRC64;
MRCLALDIGG TKIAAAIVKN GEIEQRQQIH TPRENVVEGM HQALGKLLAD YEGQFDYVAV
ASTGIINNGI LSALNPKNLG GLAEFPLKAS IAKHTDKPIG LLNDAQAATY AEYQLQNFEQ
VSNFVFITVS TGVGGGIVLN QILQTGSRGI AGHIGHTLAD PNGAICGCGR RGCVEAIASG
RAIEAVSSQW EDPCDPKEVF ERFRKNDEKA TALVERSAKA IANLIADLVI SLDIQKIAIG
GSVGLAEGYL SLVEKYLQDF PSIYCCEIET AKFGQDAGLI GAAYWVKDVL LDKPEGTIYG
