ID A4CUM9_SYNPV Unreviewed; 594 AA.
AC A4CUM9;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
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=WH7805_02877 {ECO:0000313|EMBL:EAR18744.1};
OS Synechococcus sp. (strain WH7805).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=59931 {ECO:0000313|EMBL:EAR18744.1, ECO:0000313|Proteomes:UP000001224};
RN [1] {ECO:0000313|EMBL:EAR18744.1, ECO:0000313|Proteomes:UP000001224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7805 {ECO:0000313|Proteomes:UP000001224};
RA Scanlan D., Ostrowski M., Mazard S., Wilkinson N., Partensky F.,
RA Dufresne A., Garczarek L., Hess W., Gierga G., Voss B., Axmann I., Post A.,
RA Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K., Beeson K.,
RA Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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 -!- 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:EAR18744.1}.
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DR EMBL; AAOK01000003; EAR18744.1; -; Genomic_DNA.
DR RefSeq; WP_006041391.1; NZ_CH724168.1.
DR AlphaFoldDB; A4CUM9; -.
DR STRING; 59931.WH7805_02877; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_2_3; -.
DR OrthoDB; 9812123at2; -.
DR PhylomeDB; A4CUM9; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000001224; 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:EAR18744.1};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:EAR18744.1}.
FT DOMAIN 8..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; 63369 MW; 2589F27BF8F023B2 CRC64;
MAVIDLNRRT KIVATIGPAT ESAERIRELI QAGATTFRLN FSHGDHSEHA TRMATIRQVA
HELGVHIGIL QDLQGPKIRL GRFEEGPITL GKGDHFSLTS KKVRCNQTVA TVTYDKLADE
VTAGSRILLD DGRVEMRVDR VDLADQTLHC VVTVGGVLSN NKGVNFPDVQ LSVRALTPKD
RQDLAFGLQQ GVDWVALSFV RNPSDMQEIR ELIRKHGFTT PVVAKIEKFE AIDQIDAILP
LCDGVMVARG DLGVEMPAEE VPLLQKDLIH KANSLGIPII TATQMLDSMA SSPRPTRAEV
SDVANAILDG TDAVMLSNET AVGDFPVEAV ETMATIARRI ERDYPQRPID THLPSTIPNA
ISGAVSSIAR QLNAAAILPL TKSGATAHNV SKFRPSTPIL AITSEVAVAR KLQLVWGVTP
LLIETQKSTT ATFTLAMGVA QEMGVLKDGD LCVQTAGTLA GVSGSTDLIK VGIVSAVLGR
GTGIGNGSIS GKVRIARTAS DCARLEPGEI LVASDTNADY LDAFREAAAI ITECGGEESH
AAVIARRLGL SVITGVANAT RDLREGEVVT LHIKEGAVHR GTGSNMLMKL DTML
//
