ID A0A1W2A013_9FLAO Unreviewed; 481 AA.
AC A0A1W2A013;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN02787074_1854 {ECO:0000313|EMBL:SMC53751.1};
OS Chryseobacterium sp. YR221.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1500293 {ECO:0000313|EMBL:SMC53751.1, ECO:0000313|Proteomes:UP000192341};
RN [1] {ECO:0000313|EMBL:SMC53751.1, ECO:0000313|Proteomes:UP000192341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR221 {ECO:0000313|EMBL:SMC53751.1,
RC ECO:0000313|Proteomes:UP000192341};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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 -!- 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}.
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DR EMBL; FWXM01000002; SMC53751.1; -; Genomic_DNA.
DR RefSeq; WP_047493496.1; NZ_FWXM01000002.1.
DR AlphaFoldDB; A0A1W2A013; -.
DR STRING; 1500293.SAMN02787074_1854; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000192341; 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; 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.
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:SMC53751.1};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 6..329
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 367..478
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 481 AA; 53664 MW; 36512AF3B4BB2FF2 CRC64;
MNKYLKKTKI IATLGPASSS KEVMLDLMKA GVDIFRINFS HADYDLVRNN IDIIRELNSE
YGYSVGILGD LQGPKLRVGV VKEGSYLNPG DILTFTNEKM EGDSTKVFMT YQQFPQDVKV
GERILIDDGK LVLEVTETNE KDTVKAKTIQ GGPLSSKKGV NLPNTKVSLP ALTEKDIQDA
NFMLDMEVDW IALSFVRHAQ DIIDLKELIA KHPNGKFKTP IIAKIEKPEG VKNIDEILLE
CDGLMVARGD LGVEVPMEEV PAIQKNLVEK ARFYSKPVII ATQMMETMIN SLTPTRAEVN
DVANSVLDGA DAVMLSGETS VGRYPVQVVE NMAKIVKNIE TTHFYQHKNE PIEKDYNCID
ERFITNRVCL AAVRIAKTTN VSAIVTLTHS GYTAFQLAAH RPNSQIIVYS GNKRVITMLN
LLWGVHAYYY DMKKSTDETI IQVNMLTHNY GYIETGDFVI NINATPSYEG GKTNTLRLTT
V
//
