ID   KPYK2_AGRVI             Reviewed;         482 AA.
AC   Q44473;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 55.
DE   RecName: Full=Pyruvate kinase;
DE            Short=PK;
DE            EC=2.7.1.40;
GN   Name=ttuE;
OS   Agrobacterium vitis (Rhizobium vitis).
OG   Plasmid pTrAB4.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX   NCBI_TaxID=373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AB4;
RX   MEDLINE=96062236; PubMed=7592429;
RA   Crouzet P., Otten L.;
RT   "Sequence and mutational analysis of a tartrate utilization operon
RT   from Agrobacterium vitis.";
RL   J. Bacteriol. 177:6518-6526(1995).
CC   -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate.
CC   -!- COFACTOR: Magnesium.
CC   -!- COFACTOR: Potassium.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- INDUCTION: By tartrate.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family.
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DR   EMBL; U25634; AAA68700.1; -; Genomic_DNA.
DR   HSSP; P14178; 1E0T.
DR   BRENDA; 2.7.1.40; 97084.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR   GO; GO:0004743; F:pyruvate kinase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR001697; Pyr_Knase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase_cat.
DR   InterPro; IPR015794; Pyrv_Knase_a/b.
DR   InterPro; IPR018209; Pyrv_Knase_AS.
DR   InterPro; IPR015793; Pyrv_Knase_brl.
DR   Gene3D; G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 1.
DR   Gene3D; G3DSA:3.40.1380.20; Pyrv_Knase_a/b; 1.
DR   PANTHER; PTHR11817; Pyruvate_kinase; 1.
DR   Pfam; PF00224; PK; 1.
DR   Pfam; PF02887; PK_C; 1.
DR   PRINTS; PR01050; PYRUVTKNASE.
DR   ProDom; PD001009; Pyruvate_kinase; 2.
DR   TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR   PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Plasmid; Pyruvate; Transferase.
FT   CHAIN         1    482       Pyruvate kinase.
FT                                /FTId=PRO_0000112052.
FT   ACT_SITE    220    220       By similarity.
FT   METAL       222    222       Magnesium (By similarity).
FT   METAL       243    243       Magnesium (By similarity).
FT   METAL       244    244       Magnesium (By similarity).
SQ   SEQUENCE   482 AA;  51678 MW;  2D2B614589CB46E7 CRC64;
     MFIRNNRRSK IVATVGPASS SPDMLRSLFL AGVDTFRLNF SHGARADHAE VYRNIRALEQ
     EHDAAIAVLQ DLQGPKIRIG VLAHGRLDLA RGSTIGFILG REGGEGMNDI PLPHREIFEV
     AVPGMDLLID DGRIKVRIME VMDGRLVCEV LNGGALSNRK GVNVPGAVLD ISPLTAKDRE
     DLEFGLELGV DWVALSFVQR ARDMIEARSL VGDRAGLIAK IEKPSALDDI EDIVRLSDSV
     MVARGDLGVE IPPEDVPGKQ KEIIRACRLA AKPVIVATQM LDSMVSSPTP TRAEASDVAG
     AIYDGADAVM LSAETATGAY PVEAVEIMNR IIEKTEKHKH YRPILEATEP DVAQSPPHAV
     ATAAANVAVA LGSPVVVAYT SSGTTAARIS RARPALPILA LTPSEQVARR LNMFWGVVGV
     RSQDVHTYEA SLIHAQQAVQ EAKLASPSDH IVIVAGFPFA QQGSTNNLRV VQIAATDNLE
     IA
//