ID A0A5Q0JTR1_9FLAO Unreviewed; 480 AA.
AC A0A5Q0JTR1;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 24-JAN-2024, entry version 13.
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:QFZ54324.1};
GN ORFNames=FEZ18_05740 {ECO:0000313|EMBL:QFZ54324.1};
OS Oceanihabitans sp. IOP_32.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Oceanihabitans.
OX NCBI_TaxID=2529032 {ECO:0000313|EMBL:QFZ54324.1, ECO:0000313|Proteomes:UP000325630};
RN [1] {ECO:0000313|EMBL:QFZ54324.1, ECO:0000313|Proteomes:UP000325630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IOP_32 {ECO:0000313|EMBL:QFZ54324.1,
RC ECO:0000313|Proteomes:UP000325630};
RA He Y., Zeng X., Xiong J., Shao Z.;
RT "Oceanihabitans indica sp. nov., isolated from the Deep sea sulfide in the
RT Southwest Indian Ocean.";
RL Submitted (MAY-2019) 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}.
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DR EMBL; CP040813; QFZ54324.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5Q0JTR1; -.
DR KEGG; oci:FEZ18_05740; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000325630; 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: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:QFZ54324.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000325630};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:QFZ54324.1}.
FT DOMAIN 5..326
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 361..472
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 480 AA; 53331 MW; FD1DF25A8D885A08 CRC64;
MLIRKKTKIV ATLGPATSTK ETLKAMLEEG VDVFRINFSH ADYKDVEARI KMIRELNDEL
GYSAAILGDL QGPKLRVGVM KEDVVVQEGD EIIFATGKRF EGTKERVFMT YERFPQDAKP
GERILLDDGK LIFEVVSTNK TTEVKARVIQ GGPLKSKKGV NLPNTAISQP ALTEKDVEDA
IFAIGQEVDW LALSFVRHAE DLLKLRDLIK EHSKHKIPII AKIEKPEAVK NIDKIISHCD
GLMVARGDLG VEVPAEEVPL IQKELVFRAK KARIPVIIAT QMMETMISSL TPTRAEVNDV
ANSVMDGADA VMLSGETSIG SYPVQVIRQM ANILKSVENS DLIKVPELPP HIRTKRYITK
SICYHAAIMA NEINAKAIST LTNSGYTAFQ ISAWRPSSHI LVFTSNKRIL TQLSLLWGVK
AFHYDKFVST DETIEDVNKI ACDKGYLQTG DMHISLAAMP IKEKGMVNTL RVTEISNCCD
//
