ID D2B8B8_STRRD Unreviewed; 476 AA.
AC D2B8B8;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 01-MAY-2013, entry version 32.
DE RecName: Full=Pyruvate kinase;
DE EC=2.7.1.40;
GN OrderedLocusNames=Sros_2953;
OS Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 /
OS NI 9100).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Streptosporangineae; Streptosporangiaceae; Streptosporangium.
OX NCBI_TaxID=479432;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100;
RX DOI=10.4056/sigs.631049;
RA Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A.,
RA Glavina Del Rio T., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Sims D., Meincke L., Brettin T., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K.,
RA Chain P., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Streptosporangium roseum type strain (NI
RT 9100T).";
RL Stand. Genomic Sci. 2:29-37(2010).
CC -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
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DR EMBL; CP001814; ACZ85908.1; -; Genomic_DNA.
DR RefSeq; YP_003338651.1; NC_013595.1.
DR ProteinModelPortal; D2B8B8; -.
DR EnsemblBacteria; ACZ85908; ACZ85908; Sros_2953.
DR GeneID; 8666239; -.
DR KEGG; sro:Sros_2953; -.
DR PATRIC; 32467883; VBIStrRos112010_2935.
DR HOGENOM; HOG000021558; -.
DR KO; K00873; -.
DR OMA; EMPLESV; -.
DR UniPathway; UPA00109; UER00188.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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-UniPathway.
DR Gene3D; 2.40.33.10; -; 1.
DR Gene3D; 3.20.20.60; -; 2.
DR Gene3D; 3.40.1380.20; -; 1.
DR InterPro; IPR001697; Pyr_Knase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom.
DR InterPro; IPR015794; Pyrv_Knase_a/b.
DR InterPro; IPR018209; Pyrv_Knase_AS.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom.
DR PANTHER; PTHR11817; PTHR11817; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF50800; PK_B_barrel_like; 1.
DR SUPFAM; SSF52935; Pyruvate_kinase; 1.
DR SUPFAM; SSF51621; Pyrv/PenolPyrv_Kinase_cat; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE 3: Inferred from homology;
KW Complete proteome; Glycolysis; Kinase; Magnesium; Pyruvate;
KW Transferase.
SQ SEQUENCE 476 AA; 51140 MW; E5193B96CA1D010A CRC64;
MTRRAKIVCT LGPATSSPER LRELIAAGMD VARFNLSHGS HELHKEVYDR VREAAAELGR
GVGVLADLQG PKIRVGKFEE GPVRLGFGDV FTVTTEEVPG DREQVSTTYL GLPNDVRPGD
SILVDDGRVH LEVTRVDGPR VTTRVIIGGM ISDNKGLNLP GVNVSAPALT DKDETDLRWA
LRTGFDLIAL SFVRRPSDAD VVRNIMEQEA VRLPLLAKIE KPQAVERLPE IIEAFDGIMV
ARGDLGVELP LEEVPIVQKR AIELCREKAR PVIVATQMLD SMISSPRPTR AEASDVAYAV
MDGADAVMLS GETSVGNYPI ESVQTMSRIA TTAEKTSLQA THSLDRLPET TGGAIARAAA
EVGAIVGAKA LVAFTMSGET ARRLARYRSP IPLLAFTSSP HVRCQLALTW GVETFEVPFV
HHTDDMVRQV EASLLANARL EKGDKVVIVA GSPPGTAGST NALRVHTIGS AVSHPA
//
