NAHK_BIFL2
ID NAHK_BIFL2 Reviewed; 359 AA.
AC E8MF12; A7BJ81;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=N-acetylhexosamine 1-kinase;
DE EC=2.7.1.162;
DE AltName: Full=N-acetylgalactosamine/N-acetylglucosamine 1-kinase;
GN Name=nahK; Synonyms=lnpB; OrderedLocusNames=BLLJ_1622;
OS Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM
OS 1217 / NCTC 11818 / E194b).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=565042;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND GENE NAME.
RC STRAIN=ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b;
RX PubMed=17720833; DOI=10.1128/aem.01425-07;
RA Nishimoto M., Kitaoka M.;
RT "Identification of N-acetylhexosamine 1-kinase in the complete lacto-N-
RT biose I/galacto-N-biose metabolic pathway in Bifidobacterium longum.";
RL Appl. Environ. Microbiol. 73:6444-6449(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b;
RX PubMed=21270894; DOI=10.1038/nature09646;
RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA Morita H., Hattori M., Ohno H.;
RT "Bifidobacteria can protect from enteropathogenic infection through
RT production of acetate.";
RL Nature 469:543-547(2011).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19683921; DOI=10.1016/j.bmcl.2009.07.104;
RA Cai L., Guan W., Wang W., Zhao W., Kitaoka M., Shen J., O'Neil C.,
RA Wang P.G.;
RT "Substrate specificity of N-acetylhexosamine kinase towards N-
RT acetylgalactosamine derivatives.";
RL Bioorg. Med. Chem. Lett. 19:5433-5435(2009).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19436918; DOI=10.1039/b904853g;
RA Cai L., Guan W., Kitaoka M., Shen J., Xia C., Chen W., Wang P.G.;
RT "A chemoenzymatic route to N-acetylglucosamine-1-phosphate analogues:
RT substrate specificity investigations of N-acetylhexosamine 1-kinase.";
RL Chem. Commun. (Camb.) 20:2944-2946(2009).
CC -!- FUNCTION: Phosphorylates both N-acetylglucosamine (GlcNAc) and N-
CC acetylgalactosamine (GalNAc) at similar rates. Involved in the lacto-N-
CC biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is
CC important for host intestinal colonization by bifidobacteria. Also
CC accepts GTP and ITP as phosphate donors. In vitro, can phosphorylate
CC several GlcNAc and GalNAc derivatives. {ECO:0000269|PubMed:17720833,
CC ECO:0000269|PubMed:19436918, ECO:0000269|PubMed:19683921}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-acetyl-D-hexosamine = ADP + H(+) + N-acetyl-alpha-D-
CC hexosamine 1-phosphate; Xref=Rhea:RHEA:25428, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:21601, ChEBI:CHEBI:30616, ChEBI:CHEBI:138007,
CC ChEBI:CHEBI:456216; EC=2.7.1.162;
CC Evidence={ECO:0000269|PubMed:17720833, ECO:0000269|PubMed:19436918,
CC ECO:0000269|PubMed:19683921};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17720833};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.118 mM for GlcNAc {ECO:0000269|PubMed:17720833};
CC KM=0.065 mM for GalNAc {ECO:0000269|PubMed:17720833};
CC KM=0.172 mM for ATP {ECO:0000269|PubMed:17720833};
CC Note=kcat is 1.21 sec(-1) for GlcNAc. kcat is 0.752 sec(-1) for
CC GalNAc.;
CC pH dependence:
CC Optimum pH is 8.5. Stable at pH 5.0 to 9.5 at 30 degrees Celsius.
CC {ECO:0000269|PubMed:17720833};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:17720833};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR EMBL; AB303839; BAF73925.1; -; Genomic_DNA.
DR EMBL; AP010888; BAJ67289.1; -; Genomic_DNA.
DR RefSeq; WP_013582917.1; NC_015067.1.
DR PDB; 4OCJ; X-ray; 1.57 A; A=1-359.
DR PDB; 4OCK; X-ray; 1.72 A; A=1-359.
DR PDB; 4OCO; X-ray; 2.16 A; A=1-359.
DR PDB; 4OCP; X-ray; 1.94 A; A=1-359.
DR PDB; 4OCQ; X-ray; 1.88 A; A=1-359.
DR PDB; 4WH1; X-ray; 2.05 A; A=1-359.
DR PDB; 4WH2; X-ray; 1.85 A; A=1-359.
DR PDB; 4WH3; X-ray; 1.80 A; A=1-359.
DR PDBsum; 4OCJ; -.
DR PDBsum; 4OCK; -.
DR PDBsum; 4OCO; -.
DR PDBsum; 4OCP; -.
DR PDBsum; 4OCQ; -.
DR PDBsum; 4WH1; -.
DR PDBsum; 4WH2; -.
DR PDBsum; 4WH3; -.
DR AlphaFoldDB; E8MF12; -.
DR SMR; E8MF12; -.
DR KEGG; blm:BLLJ_1622; -.
DR HOGENOM; CLU_037718_0_0_11; -.
DR OMA; DCLRSCC; -.
DR BioCyc; MetaCyc:MON-13865; -.
DR BRENDA; 2.7.1.162; 851.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; Kinase; Magnesium;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..359
FT /note="N-acetylhexosamine 1-kinase"
FT /id="PRO_0000424071"
FT DOMAIN 21..359
FT /note="Protein kinase"
FT CONFLICT 7
FT /note="D -> V (in Ref. 1; BAF73925)"
FT /evidence="ECO:0000305"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:4OCJ"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:4OCJ"
FT STRAND 31..42
FT /evidence="ECO:0007829|PDB:4OCJ"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:4OCJ"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:4OCJ"
FT HELIX 58..73
FT /evidence="ECO:0007829|PDB:4OCJ"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:4OCJ"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:4OCJ"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:4OCJ"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:4OCJ"
FT HELIX 117..134
FT /evidence="ECO:0007829|PDB:4OCJ"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4OCJ"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:4OCJ"
FT HELIX 152..165
FT /evidence="ECO:0007829|PDB:4OCJ"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:4OCJ"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:4OCJ"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:4OCJ"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:4OCJ"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:4OCK"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:4OCJ"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:4OCJ"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:4OCJ"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:4OCJ"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:4OCJ"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:4OCK"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:4OCJ"
FT HELIX 237..248
FT /evidence="ECO:0007829|PDB:4OCJ"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:4OCJ"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:4OCJ"
FT HELIX 266..280
FT /evidence="ECO:0007829|PDB:4OCJ"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:4OCJ"
FT HELIX 286..313
FT /evidence="ECO:0007829|PDB:4OCJ"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:4OCK"
FT HELIX 325..342
FT /evidence="ECO:0007829|PDB:4OCJ"
FT HELIX 344..354
FT /evidence="ECO:0007829|PDB:4OCJ"
SQ SEQUENCE 359 AA; 39903 MW; FBC9DD776E6BA5A3 CRC64;
MTESNEDLFG IASHFALEGA VTGIEPYGDG HINTTYLVTT DGPRYILQQM NTSIFPDTVN
LMRNVELVTS TLKAQGKETL DIVPTTSGAT WAEIDGGAWR VYKFIEHTVS YNLVPNPDVF
REAGSAFGDF QNFLSEFDAS QLTETIAHFH DTPHRFEDFK AALAADKLGR AAACQPEIDF
YLSHADQYAV VMDGLRDGSI PLRVTHNDTK LNNILMDATT GKARAIIDLD TIMPGSMLFD
FGDSIRFGAS TALEDEKDLS KVHFSTELFR AYTEGFVGEL RGSITAREAE LLPFSGNLLT
MECGMRFLAD YLEGDIYFAT KYPEHNLVRT RTQIKLVQEM EQKASETRAI VADIMEAAR
