ID A0A2P7N261_9CYAN Unreviewed; 594 AA.
AC A0A2P7N261;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
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 Name=pyk {ECO:0000313|EMBL:PSJ07556.1};
GN ORFNames=C7K55_01630 {ECO:0000313|EMBL:PSJ07556.1};
OS Cyanobium usitatum str. Tous.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Cyanobium.
OX NCBI_TaxID=2116684 {ECO:0000313|EMBL:PSJ07556.1, ECO:0000313|Proteomes:UP000243002};
RN [1] {ECO:0000313|EMBL:PSJ07556.1, ECO:0000313|Proteomes:UP000243002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tous {ECO:0000313|EMBL:PSJ07556.1,
RC ECO:0000313|Proteomes:UP000243002};
RX PubMed=30117250; DOI=.1111/1462-2920.14377;
RA Cabello-Yeves P.J., Picazo A., Camacho A., Callieri C., Rosselli R.,
RA Roda-Garcia J.J., Coutinho F.H., Rodriguez-Valera F.;
RT "Ecological and genomic features of two widespread freshwater
RT picocyanobacteria.";
RL Environ. Microbiol. 20:3757-3771(2018).
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 -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PEP-utilizing
CC enzyme family. {ECO:0000256|ARBA:ARBA00006237}.
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:PSJ07556.1}.
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DR EMBL; PXXO01000001; PSJ07556.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7N261; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000243002; 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; 3.50.30.10; Phosphohistidine domain; 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; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
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; 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; PF00391; PEP-utilizers; 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; SSF52009; Phosphohistidine domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF52935; PK C-terminal domain-like; 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 Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:PSJ07556.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243002};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 7..330
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 359..471
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT DOMAIN 505..576
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 594 AA; 63258 MW; 142F4B394860D80D CRC64;
MPQPDLMRRT KIVATIGPAT ESAERLRELV AAGATTFRLN FSHGDHSEHA ARIATIRQVS
TELGIELGIL QDLQGPKIRL GRFADGPITL AKGDQFTLTS RDVPCNQKIA TVTYASLADE
VVPGSRILLD DGRVEMVVES VDKPEQTLFC SVTVGGVLSN NKGVNFPDVQ LSIRALTEKD
RVDLAFGLKQ GVDWVALSFV RNPSDMREIR ELIRSHGHDT PVVAKIEKFE AIDQIDDILP
LCDGVMVARG DLGVEMPAEE VPLLQKELIR KANSLGIPVI TATQMLDSMV SCPRPTRAEV
SDVANAILDG TDAVMLSNES AVGDFPVEAV ATMAIIARRI ERDYPRRVLD SHMATTIPNA
ICQAVSSIAR QLNAAAILPL TKGGSTARSV SKFRPSTPIL AITSEVNVAR QLQLCWGVNP
LVVEEQSSST STFSLAMGMA RELGFLRDGD LVVQTAGTLS GISGSTDFIK VGIVSAVLSK
GTGVGTGSVS GRVRLVDSPE AAAAIQSGEI LVVHETCADY VEAIRKAKGV VTEAGGLESH
AALIAERTGV PTIVGVCNAI ANLRQGEIVT LDLQRGEVHR GARSHDADDK PAIV
//
