NANK_VIBVU
ID NANK_VIBVU Reviewed; 293 AA.
AC Q8D612;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=VV2_0735;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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; AE016796; AAO07667.1; -; Genomic_DNA.
DR RefSeq; WP_011081664.1; NC_004460.2.
DR AlphaFoldDB; Q8D612; -.
DR SMR; Q8D612; -.
DR EnsemblBacteria; AAO07667; AAO07667; VV2_0735.
DR KEGG; vvu:VV2_0735; -.
DR HOGENOM; CLU_036604_0_4_6; -.
DR OMA; APNIDWR; -.
DR UniPathway; UPA00629; UER00681.
DR Proteomes; UP000002275; Chromosome 2.
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 3: Inferred from homology;
KW ATP-binding; Carbohydrate metabolism; Kinase; Metal-binding;
KW Nucleotide-binding; Transferase; Zinc.
FT CHAIN 1..293
FT /note="N-acetylmannosamine kinase"
FT /id="PRO_0000095705"
FT BINDING 5..12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT BINDING 133..140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
SQ SEQUENCE 293 AA; 30968 MW; B2F3AF6F6197DAEF CRC64;
MKVLAIDIGG TKIALGNVVE GHLQHRKQFP TPVVNDATTL AKEILAHCQA WLSDVDAIGI
STTGLVSEQG ISAINPGTLS FPTPFPLHSE LHRLSGKPVK MLNDAQAAAW YEFLQLSPEL
DVRNMAYITV STGVGGGLVI NQQLHKGKSN FAGHIGHTVL DPNGPLCGCQ QRGCVEAIAS
GNAINAGAQA LFGQAISNIE LFQLAQHNEQ ASTLIQQSAE AIAQLCLNLK ATLDLDLVVI
GGGVGLARGY LARVQAFIDK QPLVFQVKVR AAVGDYDACL LGAAFQFEES NLS