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Database: UniProt
Entry: A0A0F5VLJ3_9ACTN
LinkDB: A0A0F5VLJ3_9ACTN
Original site: A0A0F5VLJ3_9ACTN 
ID   A0A0F5VLJ3_9ACTN        Unreviewed;       474 AA.
AC   A0A0F5VLJ3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
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   ORFNames=TN53_37855 {ECO:0000313|EMBL:KKD02918.1};
OS   Streptomyces sp. WM6386.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415558 {ECO:0000313|EMBL:KKD02918.1, ECO:0000313|Proteomes:UP000033641};
RN   [1] {ECO:0000313|EMBL:KKD02918.1, ECO:0000313|Proteomes:UP000033641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM6386 {ECO:0000313|EMBL:KKD02918.1,
RC   ECO:0000313|Proteomes:UP000033641};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (JAN-2015) 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:KKD02918.1}.
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DR   EMBL; JXTE01000104; KKD02918.1; -; Genomic_DNA.
DR   RefSeq; WP_046263381.1; NZ_JXTE01000104.1.
DR   AlphaFoldDB; A0A0F5VLJ3; -.
DR   PATRIC; fig|1415558.3.peg.497; -.
DR   OrthoDB; 9812123at2; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000033641; 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:KKD02918.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033641};
KW   Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:KKD02918.1}.
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   474 AA;  51159 MW;  1E35D50E8DBEE8BB CRC64;
     MRRSKIVCTL GPAVDSHEML VSLIEAGMNV ARFNFSHGTH AEHQGRYDRV RAAAKETGRA
     IGVLADLQGP KIRLETFAEG PVELERGDEF VITTEDVPGD KQICGTTYKG LPGDVSRGDQ
     ILINDGNVEL KVLDVEGPRV KAIVIEGGVV SDHKGINLPG AAVNVPALSE KDVEDLRFAL
     RMGADMVALS FVRDAKDVAD VHKVMDEEGR RVPVIAKVEK PQAVENMEDV VMAFDAVMVA
     RGDLAVEYPL EKVPMVQKRL IELCRRNAKP VIVATQMMES MITNSRPTRA EASDVANAIL
     DGADAVMLSA ESSVGAYPIE TVKTMSKIVT AAEQELLSKG LQPLVPGKKP RTQGGSIARA
     ACEIADFLGG RGLVAFTQSG DTARRLSRYR AVQPIVAFTT DESTRNQLTL SWGVESHVVP
     FVNSTDEMVD MVDQEIAKIN RFNPGEIVII TAGSPPGIPG TTNMLRVHHL GGQK
//
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