ID A0A0M2Q1S0_PROHO Unreviewed; 475 AA.
AC A0A0M2Q1S0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN ORFNames=PROH_10785 {ECO:0000313|EMBL:KKJ00572.1};
OS Prochlorothrix hollandica PCC 9006 = CALU 1027.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Prochlorotrichales;
OC Prochlorotrichaceae; Prochlorothrix.
OX NCBI_TaxID=317619 {ECO:0000313|EMBL:KKJ00572.1, ECO:0000313|Proteomes:UP000034681};
RN [1] {ECO:0000313|EMBL:KKJ00572.1, ECO:0000313|Proteomes:UP000034681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CALU 1027 {ECO:0000313|EMBL:KKJ00572.1};
RA Shanker A., Yadav P., Khan S., Sharma V.;
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKJ00572.1, ECO:0000313|Proteomes:UP000034681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CALU 1027 {ECO:0000313|EMBL:KKJ00572.1};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-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 -!- 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}.
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:KKJ00572.1}.
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DR EMBL; AJTX02000004; KKJ00572.1; -; Genomic_DNA.
DR RefSeq; WP_026099315.1; NZ_KB235933.1.
DR AlphaFoldDB; A0A0M2Q1S0; -.
DR STRING; 317619.GCA_000332315_00926; -.
DR eggNOG; COG0469; Bacteria.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000034681; 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; 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:KKJ00572.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034681};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 6..328
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 357..470
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 475 AA; 51556 MW; 719D08F26BD2902F CRC64;
MKPLTHRTKV VATIGPASSS PEVIRSMVLA GMNVARLNFS HGSYADHAQI VSTLRQISEE
LDTPITLLQD LQGPKIRIGQ LPDGEVELVK GESLTLVPVE EYSGAPQTVG IDYPYLAQEA
TLGTQVLLDD GLLELTVIGV MGSAVQCQVV EGGMLKSRKG VNVPSLNLQL PSMTEKDQQD
LEFGLAQGID WVSLSFVRTA EDILTLKRFL ADRDASDVPV MAKIEKPQAI ANLDAIIQVC
DGLMVARGDL GVEMSPERVP VLQKRIIRAC NLISMPVITA TQMLDSMIRN PRPTRAEASD
VANAILDGTD AVMLSGESAV GDYPVKAVEM LVKIAHDVEE DINFVNNPPA ETDETHALSE
ALNTIDHILN LKCIVAFTTT GYTAMIAAGE RPKAPVIALT PHPKVYHRLN LVWGVKPVLL
DLTLTSFEEE IEQVEKCLLM RHLAEKGDQV LILGGTPAYR PQSTNFMKLH RVGSA
//
