ID W5W9A9_9PSEU Unreviewed; 598 AA.
AC W5W9A9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=pyruvate kinase {ECO:0000256|ARBA:ARBA00012142};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142};
GN ORFNames=KALB_4183 {ECO:0000313|EMBL:AHH97547.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH97547.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHH97547.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH97547.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663}.
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DR EMBL; CP007155; AHH97547.1; -; Genomic_DNA.
DR RefSeq; WP_025357619.1; NZ_CP007155.1.
DR AlphaFoldDB; W5W9A9; -.
DR STRING; 1449976.KALB_4183; -.
DR KEGG; kal:KALB_4183; -.
DR PATRIC; fig|1449976.3.peg.4214; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_6_1_11; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000019225; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1.
DR InterPro; IPR001697; Pyr_Knase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR PANTHER; PTHR11817:SF76; PLASTIDIAL PYRUVATE KINASE 4, CHLOROPLASTIC; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR Pfam; PF00224; PK; 2.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW Reference proteome {ECO:0000313|Proteomes:UP000019225};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 131..219
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 322..558
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
SQ SEQUENCE 598 AA; 65644 MW; 1C9CF839ECDDDDCD CRC64;
MCSDTDKWVR LRSDLEALTV ALADAEEQWS SWLAAVEPGQ LGSARNLVHY WAIRQRDLRD
LQLRLAALGL SSLGRSEPHV AATLYAVERA VYALSGMPWR SCRRAAAQPG EGSRWLTDRA
ADLLGPVAPG RRARVMVTLP SSAADDPDLA RRLLARGMRL ARINCAHDDA DAWRRMTHNV
REAARSASGD CRIVMDLAGP KLRTGPLAPG PKVVRLRPTR DLLGRVTAPA RCWLTPAERR
MAPPDPRMTS VPVPMAWLLA RRDGETVTVR DTRGANRALV LARCGDGMIA TVERTTYLAT
GTPLADSCTV GELPAVEQRL LLRAGDVLEL TKDCAPAPVG PGQLRIGCTL PEAIEHAEVG
QPVHIDDGKI SGRVIARTPE LLKVRITRAG PNGSRLAGGR GVNLPETRLP VSALSSKDLA
DLPTVLDLAD VVELSFVRDA TDVEQLFGEL DRLGDDRVGV VLKIETKQAF ERLPQVLLTA
MRRPRVGVMI ARGDLAVECG YERLAELQEE ILWLCEAAHL PVIWATQVLE QLARRGRPSR
AEISDAAMSE RAECVMLNKG PYIEEAVSTL DNVLRRMSRH HYKKNALLQS LHSWRPDQ
//