NANK_HAEIN
ID NANK_HAEIN Reviewed; 300 AA.
AC P44541;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=N-acetylmannosamine kinase;
DE EC=2.7.1.60;
DE AltName: Full=ManNAc kinase;
DE AltName: Full=N-acetyl-D-mannosamine kinase;
GN Name=nanK; OrderedLocusNames=HI_0144;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=10675023;
RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA Fountoulakis M.;
RT "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL Electrophoresis 21:411-429(2000).
CC -!- FUNCTION: Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc)
CC to ManNAc-6-P. {ECO:0000250}.
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;
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 2/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. NanK subfamily.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC21816.1; -; Genomic_DNA.
DR PIR; H64050; H64050.
DR RefSeq; NP_438313.1; NC_000907.1.
DR RefSeq; WP_005648623.1; NC_000907.1.
DR AlphaFoldDB; P44541; -.
DR SMR; P44541; -.
DR STRING; 71421.HI_0144; -.
DR EnsemblBacteria; AAC21816; AAC21816; HI_0144.
DR KEGG; hin:HI_0144; -.
DR PATRIC; fig|71421.8.peg.146; -.
DR eggNOG; COG1940; Bacteria.
DR HOGENOM; CLU_036604_0_4_6; -.
DR OMA; APNIDWR; -.
DR PhylomeDB; P44541; -.
DR BioCyc; HINF71421:G1GJ1-156-MON; -.
DR UniPathway; UPA00629; UER00681.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009384; F:N-acylmannosamine kinase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 ATP-binding; Carbohydrate metabolism; Kinase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT CHAIN 1..300
FT /note="N-acetylmannosamine kinase"
FT /id="PRO_0000095699"
FT BINDING 5..12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 132..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 300 AA; 31918 MW; 8EDCF138D6EDC533 CRC64;
MRCLALDIGG TKIAAAIVKN GEIEQRQQIH TPRENVVEGM HQALGKLLAD YEGQFDYVAV
ASTGIINNGI LSALNPKNLG GLAEFPLKAS IAKHTDKPIG LLNDAQAATY AEYQLQNSEQ
VSNFVFITVS TGVGGGIVLN QILQTGSRGI AGHIGHTLAD PNGAICGCGR RGCVEAIASG
RAIEAVSSQW EEPCDPKEVF ERFRKNDEKA TALVERSAKA IANLIADLVI SLDIQKIAIG
GSVGLAEGYL SLVEKYLQDF PSIYCCEIET AKFGQDAGLI GAAYWVKDVL LDKPEGTIYG
