ID G5LUA3_SALET Unreviewed; 291 AA.
AC G5LUA3;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=N-acetylmannosamine kinase {ECO:0000256|HAMAP-Rule:MF_01234};
DE EC=2.7.1.60 {ECO:0000256|HAMAP-Rule:MF_01234};
DE AltName: Full=ManNAc kinase {ECO:0000256|HAMAP-Rule:MF_01234};
DE AltName: Full=N-acetyl-D-mannosamine kinase {ECO:0000256|HAMAP-Rule:MF_01234};
GN Name=nanK {ECO:0000256|HAMAP-Rule:MF_01234};
GN ORFNames=LTSEALA_4764 {ECO:0000313|EMBL:EHC32257.1};
OS Salmonella enterica subsp. enterica serovar Alachua str. R6-377.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913241 {ECO:0000313|EMBL:EHC32257.1, ECO:0000313|Proteomes:UP000004642};
RN [1] {ECO:0000313|EMBL:EHC32257.1, ECO:0000313|Proteomes:UP000004642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R6-377 {ECO:0000313|EMBL:EHC32257.1,
RC ECO:0000313|Proteomes:UP000004642};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
CC -!- FUNCTION: Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc)
CC to ManNAc-6-P. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01234}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01234}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. NanK subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01234}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHC32257.1}.
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DR EMBL; AFCJ01002057; EHC32257.1; -; Genomic_DNA.
DR AlphaFoldDB; G5LUA3; -.
DR PATRIC; fig|913241.3.peg.3619; -.
DR UniPathway; UPA00629; UER00681.
DR Proteomes; UP000004642; Unassembled WGS sequence.
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 CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 2.
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:SF177; N-ACETYLMANNOSAMINE KINASE; 1.
DR PANTHER; PTHR18964; ROK (REPRESSOR, ORF, KINASE) FAMILY; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR PROSITE; PS01125; ROK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01234};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_01234};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01234};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01234};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01234};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01234}; Zinc {ECO:0000256|HAMAP-Rule:MF_01234}.
FT BINDING 5..12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01234"
FT BINDING 132..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01234"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01234"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01234"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01234"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01234"
SQ SEQUENCE 291 AA; 30132 MW; 7ECD703A8BE2136E CRC64;
MTTLAIDIGG TKLAAALIDK NLRISQRREL PTPASKTPDA LREALKALVE PLRAEARQVA
IASTGIIQEG MLLALNPHNL GGLLHFPLVQ TLETIAGLPT LAVNDAQAAA WAEYHALPDD
IRDIVFITVS TGVGGGVVCD GKLLTGKGGL AGHLGHTLAD PHGPVCGCGR VGCVEAIASG
RGMAAAARDD LAGCDAKTLF IRAGEGHQQA RHLVSQSAQV IARMIADVKA TTDCQCVVIG
GSVGLAEGYL EQVRAFLMQE PVPYHVALSA ARYRHDAGLL GAALLAQGDT L
//
