ID A0A1I6W0R7_9ACTN Unreviewed; 476 AA.
AC A0A1I6W0R7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:QKV70959.1};
GN ORFNames=HUT13_20975 {ECO:0000313|EMBL:QKV70959.1},
GN SAMN05444716_111114 {ECO:0000313|EMBL:SFT19597.1};
OS Streptomyces harbinensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1176198 {ECO:0000313|EMBL:SFT19597.1, ECO:0000313|Proteomes:UP000198873};
RN [1] {ECO:0000313|Proteomes:UP000198873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7047 {ECO:0000313|Proteomes:UP000198873};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SFT19597.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7047 {ECO:0000313|EMBL:SFT19597.1};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QKV70959.1, ECO:0000313|Proteomes:UP000509706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA02264 {ECO:0000313|EMBL:QKV70959.1,
RC ECO:0000313|Proteomes:UP000509706};
RA Zhang B., Shi J., Ge H.;
RT "Genome mining for natural products.";
RL Submitted (JUN-2020) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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DR EMBL; CP054938; QKV70959.1; -; Genomic_DNA.
DR EMBL; FPAB01000011; SFT19597.1; -; Genomic_DNA.
DR RefSeq; WP_019434361.1; NZ_FPAB01000011.1.
DR AlphaFoldDB; A0A1I6W0R7; -.
DR STRING; 1176198.SAMN05444716_111114; -.
DR KEGG; shar:HUT13_20975; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000198873; Unassembled WGS sequence.
DR Proteomes; UP000509706; 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 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; PYRUVATE KINASE; 1.
DR PANTHER; PTHR11817:SF132; PYRUVATE KINASE 1; 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:SFT19597.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198873};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:QKV70959.1}.
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; 51743 MW; A36E3E8B45BCDAD9 CRC64;
MRRSKIVCTL GPAVDSYEQL KALIDAGMNV ARFNFSHGSH QEHEERYHRL RKASEDCGVA
VGVLADLQGP KIRLETFADG PVELERGDEF TITTEDVAGD KHICGTTYKG LPGDVAKGET
ILINDGNVSL QVLEVDGPRV RTIVIEGGVI SDHKGINLPG IAVNVPALSE KDVEDLEFAL
RLGADMVALS FVRDADDVRD VHEVMDRVGR RVPVIAKVEK PQAVENMEEV VLAFDAVMVA
RGDLAVEYPL EKVPLVQKRL IDLCRRNAKP VIVATQMMES MITNSRPTRA EASDVANAIL
DGADAVMLSA ESSVGRYPIE TVKTMSKIAI AAEEQLLSRG LQPLVPGKKP RTQGGSVARA
ACEMADFLDA KSLVAFTKSG DTARRLSRYR AVQPILAFTT DPSTRNQLTL TWGVETFVVP
WVSHTDEMVE LVDAELLKLN RYHRGDTMII TAGSPPGVAG TTNMVRVHHL GGQQGV
//
