NADK_YERPE
ID NADK_YERPE Reviewed; 293 AA.
AC Q8ZH09; Q0WHT9;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=NAD kinase {ECO:0000255|HAMAP-Rule:MF_00361};
DE EC=2.7.1.23 {ECO:0000255|HAMAP-Rule:MF_00361};
DE AltName: Full=ATP-dependent NAD kinase {ECO:0000255|HAMAP-Rule:MF_00361};
GN Name=nadK {ECO:0000255|HAMAP-Rule:MF_00361};
GN OrderedLocusNames=YPO1106, y3074, YP_1050;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS), AND SUBUNIT.
RG Center for structural genomics of infectious diseases (CSGID);
RT "Crystal structure of inorganic polyphosphate/ATP-NAD kinase from Yersinia
RT pestis CO92.";
RL Submitted (SEP-2012) to the PDB data bank.
CC -!- FUNCTION: Involved in the regulation of the intracellular balance of
CC NAD and NADP, and is a key enzyme in the biosynthesis of NADP.
CC Catalyzes specifically the phosphorylation on 2'-hydroxyl of the
CC adenosine moiety of NAD to yield NADP. {ECO:0000255|HAMAP-
CC Rule:MF_00361}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + NAD(+) = ADP + H(+) + NADP(+); Xref=Rhea:RHEA:18629,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:456216; EC=2.7.1.23;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00361};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00361};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00361}.
CC -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00361}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS61300.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL19772.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM86624.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS61300.1; ALT_INIT; Genomic_DNA.
DR PIR; AB0136; AB0136.
DR RefSeq; WP_002210719.1; NZ_WUCM01000016.1.
DR RefSeq; YP_002346149.1; NC_003143.1.
DR PDB; 4HAO; X-ray; 2.55 A; A/B=1-293.
DR PDBsum; 4HAO; -.
DR AlphaFoldDB; Q8ZH09; -.
DR SMR; Q8ZH09; -.
DR IntAct; Q8ZH09; 1.
DR STRING; 214092.YPO1106; -.
DR PaxDb; Q8ZH09; -.
DR DNASU; 1148021; -.
DR EnsemblBacteria; AAM86624; AAM86624; y3074.
DR EnsemblBacteria; AAS61300; AAS61300; YP_1050.
DR GeneID; 57977242; -.
DR KEGG; ype:YPO1106; -.
DR KEGG; ypk:y3074; -.
DR KEGG; ypm:YP_1050; -.
DR PATRIC; fig|214092.21.peg.1398; -.
DR eggNOG; COG0061; Bacteria.
DR HOGENOM; CLU_008831_0_1_6; -.
DR OMA; VNLGHVG; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProt.
DR GO; GO:0003951; F:NAD+ kinase activity; IBA:GO_Central.
DR GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR GO; GO:0006741; P:NADP biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.200.30; -; 1.
DR Gene3D; 3.40.50.10330; -; 1.
DR HAMAP; MF_00361; NAD_kinase; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_C.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002504; NADK.
DR Pfam; PF01513; NAD_kinase; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; NAD; NADP;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..293
FT /note="NAD kinase"
FT /id="PRO_0000120695"
FT ACT_SITE 74
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 74..75
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 148..149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 178
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 189..194
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 248
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT SITE 176
FT /note="Responsible for conferring strict specificity to
FT NAD"
FT /evidence="ECO:0000250"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:4HAO"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:4HAO"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:4HAO"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:4HAO"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:4HAO"
FT HELIX 58..64
FT /evidence="ECO:0007829|PDB:4HAO"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:4HAO"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:4HAO"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:4HAO"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:4HAO"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:4HAO"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:4HAO"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:4HAO"
FT STRAND 122..135
FT /evidence="ECO:0007829|PDB:4HAO"
FT STRAND 142..156
FT /evidence="ECO:0007829|PDB:4HAO"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:4HAO"
FT STRAND 170..183
FT /evidence="ECO:0007829|PDB:4HAO"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:4HAO"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:4HAO"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:4HAO"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:4HAO"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:4HAO"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:4HAO"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:4HAO"
FT STRAND 258..273
FT /evidence="ECO:0007829|PDB:4HAO"
FT HELIX 278..286
FT /evidence="ECO:0007829|PDB:4HAO"
SQ SEQUENCE 293 AA; 32398 MW; C0231F341E8F4A1E CRC64;
MNNRRFDCIG IVGHPRHPAA LATHEILYHW LKARGYAVMV EQQIAHDLNL TDAITGSLAD
IGQKADLAVV VGGDGNMLGA ARVLARYDIK VIGVNRGNLG FLTDLDPDNA LQQLSDVLEG
EYLSEQRFLL ETHVRRTNQQ SRISTAINEV VLHPGKVAHM IEFEVYIDDR FAFSQRSDGL
IIATPTGSTA YSLSAGGPIL TPTLDAIVLV PMFPHTLTAR PLVISSSSTI RLKFSHITSD
LEISCDSQIA LPIQEGEEVL IRRSDFHLNL IHPKDYSYFN TLSTKLGWSK KLF
