ID A0A4Q6IFY4_9ACTN Unreviewed; 476 AA.
AC A0A4Q6IFY4;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00018587, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN Name=pyk {ECO:0000313|EMBL:RZB16590.1};
GN ORFNames=StrepF001_25215 {ECO:0000313|EMBL:RZB16590.1};
OS Streptomyces sp. F001.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1510026 {ECO:0000313|EMBL:RZB16590.1, ECO:0000313|Proteomes:UP000293662};
RN [1] {ECO:0000313|EMBL:RZB16590.1, ECO:0000313|Proteomes:UP000293662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F001 {ECO:0000313|EMBL:RZB16590.1,
RC ECO:0000313|Proteomes:UP000293662};
RA Braesel J., Clark C.M., Kunstman K.J., Green S.J., Maienschein-Cline M.,
RA Murphy B.T., Eustaquio A.S.;
RT "Genome sequence of marine-derived Streptomyces sp. F001, a producer of
RT akashin A and diazaquinomycins.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=2.7.1.40; Evidence={ECO:0000256|RuleBase:RU000504};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997,
CC ECO:0000256|RuleBase:RU000504}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RZB16590.1}.
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DR EMBL; QZWF01000007; RZB16590.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q6IFY4; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000293662; Unassembled WGS sequence.
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 Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 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; IPR018209; Pyrv_Knase_AS.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR036918; Pyrv_Knase_C_sf.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR NCBIfam; TIGR01064; pyruv_kin; 1.
DR PANTHER; PTHR11817:SF3; AT14039P-RELATED; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF52935; PK C-terminal domain-like; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000504};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000504};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000504};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:RZB16590.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000293662};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:RZB16590.1}.
FT DOMAIN 1..322
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 356..468
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 476 AA; 51173 MW; B7A82BE9B8061431 CRC64;
MRRSKIVCTL GPAVDSHEQL VALIEAGMSV ARFNFSHGTH AEHQGRYDRV RAAAKETGRA
VGVLADLQGP KIRLATFAEG PVELVRGDEF TITTEDVPGD KTICGTTYKG LPGDVARGDQ
ILINDGNVEL KVLDVEGARV RTIVIEGGVI SDHKGINLPG AAVNVPALSE KDVEDLRFAL
RMGCDLVALS FVRDAKDVHD VHRVMDEEGR RVPVIAKVEK PQAVANMEDV VMAFDGVMVA
RGDLAVEYPL EKVPMVQKRL IELCRRNAKP VIVATQMMES MITNSRPTRA EASDVANAIL
DGADAVMLSA ESSVGAYPIE TVKTMSKIVQ AAEQELLSKG LQPLVPGKKP RTQGGSVARA
ACEIADFLGG KGLVAFTQSG DTARRLCRYR AAQPILAFTT DESTRNQLTL SWGVESHVVP
FVNSTDEMVD LVDQEIAKLN RFDAGDIMII TAGSPPGVPG TTNMVRVHHL GGGDRD
//