ID A0A1E1F6I7_9SPHN Unreviewed; 483 AA.
AC A0A1E1F6I7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SCLO_1030930 {ECO:0000313|EMBL:BAV66133.1};
OS Sphingobium cloacae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=120107 {ECO:0000313|EMBL:BAV66133.1, ECO:0000313|Proteomes:UP000218272};
RN [1] {ECO:0000313|EMBL:BAV66133.1, ECO:0000313|Proteomes:UP000218272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10874 {ECO:0000313|EMBL:BAV66133.1,
RC ECO:0000313|Proteomes:UP000218272};
RA Ootsuka M., Nishizawa T., Ohta H.;
RT "Complete Genome Sequence of the Nonylphenol-Degrading Bacterium
RT Sphingobium cloacae JCM 10874T.";
RL Submitted (OCT-2016) 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; AP017655; BAV66133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E1F6I7; -.
DR KEGG; sclo:SCLO_1030930; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000218272; 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; 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:BAV66133.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218272};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 9..326
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"
SQ SEQUENCE 483 AA; 51879 MW; E8B60D56F8347DE3 CRC64;
MTRLPPRSRK VRILATLGPA SDTPEMIRAL FVAGADAFRI NMSHGAHEDH AARIAAIRAL
EKEFGRPTTI LGDLQGPKLR VGTFARGLAV LKTGARFTLD RDEKPGDAKR VNLPHPEIYA
ALVPETRLLL DDGKLVLRVK AVMDDRIETV VEVGGALSNR KGVNVPDVVV PVPALTEKDR
RDLSFAIEQG LDWIALSFVQ RPEDLAEARR LMGGHGALMA KIEKPAAVQR LEEILELADG
VMVARGDLGV ELPPQAVPPL QKQIVATARR MGRPVVVATQ MLESMIKAPT PTRAEVSDVA
TAVYDGADAI MLSAETAAGD WPQEAVAMMD SIAHSVERDP GYFARLHFTE TRPDGTTADA
LAEGAGGIVS VVGASAITCY TTSGSTVRRV ARERPLVSIL ALTPRLDTAR KLGLTWGVHA
VRTKDVGNFE EMVGKARRMA LRHAMVEKGG KIVVLAGVPF GTPGSTNVLH VAAIRGDELR
GRE
//
