GLXK_NEIMA
ID GLXK_NEIMA Reviewed; 371 AA.
AC P57098; A1IS73;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Glycerate kinase;
DE EC=2.7.1.31;
GN Name=glxK; OrderedLocusNames=NMA1473;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RG New York structural genomics research consortium (NYSGRC);
RT "Glycerate kinase from Neisseria meningitidis (serogroup A).";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + ATP = (2R)-3-phosphoglycerate + ADP + H(+);
CC Xref=Rhea:RHEA:23516, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216;
CC EC=2.7.1.31;
CC -!- SIMILARITY: Belongs to the glycerate kinase type-1 family.
CC {ECO:0000305}.
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DR EMBL; AL157959; CAM08628.1; -; Genomic_DNA.
DR PIR; D81838; D81838.
DR RefSeq; WP_002246235.1; NC_003116.1.
DR PDB; 1TO6; X-ray; 2.50 A; A/B=1-371.
DR PDBsum; 1TO6; -.
DR AlphaFoldDB; P57098; -.
DR SMR; P57098; -.
DR EnsemblBacteria; CAM08628; CAM08628; NMA1473.
DR KEGG; nma:NMA1473; -.
DR HOGENOM; CLU_028255_0_0_4; -.
DR OMA; YTAVHEK; -.
DR BioCyc; NMEN122587:NMA_RS07370-MON; -.
DR EvolutionaryTrace; P57098; -.
DR Proteomes; UP000000626; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008887; F:glycerate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0031388; P:organic acid phosphorylation; IEA:InterPro.
DR Gene3D; 3.40.50.10350; -; 1.
DR Gene3D; 3.90.1510.10; -; 1.
DR InterPro; IPR018193; Glyc_kinase_flavodox-like_fold.
DR InterPro; IPR004381; Glycerate_kinase.
DR InterPro; IPR018197; Glycerate_kinase_RE-like.
DR InterPro; IPR036129; Glycerate_kinase_sf.
DR PANTHER; PTHR21599; PTHR21599; 1.
DR Pfam; PF02595; Gly_kinase; 1.
DR PIRSF; PIRSF006078; GlxK; 1.
DR SUPFAM; SSF110738; SSF110738; 1.
DR TIGRFAMs; TIGR00045; TIGR00045; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..371
FT /note="Glycerate kinase"
FT /id="PRO_0000071537"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1TO6"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1TO6"
FT HELIX 16..30
FT /evidence="ECO:0007829|PDB:1TO6"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1TO6"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1TO6"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:1TO6"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:1TO6"
FT STRAND 70..87
FT /evidence="ECO:0007829|PDB:1TO6"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:1TO6"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1TO6"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:1TO6"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:1TO6"
FT HELIX 141..145
FT /evidence="ECO:0007829|PDB:1TO6"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1TO6"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1TO6"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:1TO6"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1TO6"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:1TO6"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:1TO6"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:1TO6"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:1TO6"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:1TO6"
FT HELIX 217..231
FT /evidence="ECO:0007829|PDB:1TO6"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:1TO6"
FT TURN 239..246
FT /evidence="ECO:0007829|PDB:1TO6"
FT HELIX 247..254
FT /evidence="ECO:0007829|PDB:1TO6"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1TO6"
FT HELIX 262..269
FT /evidence="ECO:0007829|PDB:1TO6"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:1TO6"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:1TO6"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:1TO6"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:1TO6"
FT TURN 292..296
FT /evidence="ECO:0007829|PDB:1TO6"
FT HELIX 298..303
FT /evidence="ECO:0007829|PDB:1TO6"
FT STRAND 312..319
FT /evidence="ECO:0007829|PDB:1TO6"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:1TO6"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:1TO6"
FT HELIX 344..367
FT /evidence="ECO:0007829|PDB:1TO6"
SQ SEQUENCE 371 AA; 39526 MW; 5359A54A1841E48C CRC64;
MKIVIAPDSF KESLTAQQVA EAIKRGFQQS IADVECLLCP VGDGGEGTVD AIRHSLDLEE
KCLQVTGSFG QKEVMRYFQK EQLALFEVAD LVGLGKIPLE KRNPLQIQTR GIGELIRHLI
SQEIKEIYIG VGGTASNDGG IGIAAGLGYQ FYDEDGNALP ACGQSLLNLA SVSTENRYKI
PEDVHIRILA DVVSPLCGHQ GATYTFGKQK GLDSTMFEVV DQAIQDFYEK VSPATLKLKG
AGAGGGIAGG LCAFAQASIV SGIDTCLDLI DFDKKVSDVD LVIVGEGRLD RQSLAGKAPI
GVAKRTPVGV PVVAICGSLV EDLPSLPFEN IQAAFSILEK SEPLEDSLKN ASLYLEHTAS
NIGHLLNMPK I
