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Database: UniProt
Entry: A0A4Q6IFY4_9ACTN
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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
//
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