ID G8QLE8_AZOOP Unreviewed; 481 AA.
AC G8QLE8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
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 OrderedLocusNames=Dsui_0052 {ECO:0000313|EMBL:AEV24477.1};
OS Azospira oryzae (strain ATCC BAA-33 / DSM 13638 / PS) (Dechlorosoma
OS suillum).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Azospira.
OX NCBI_TaxID=640081 {ECO:0000313|EMBL:AEV24477.1, ECO:0000313|Proteomes:UP000005633};
RN [1] {ECO:0000313|EMBL:AEV24477.1, ECO:0000313|Proteomes:UP000005633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-33 / DSM 13638 / PS
RC {ECO:0000313|Proteomes:UP000005633};
RX PubMed=22535943; DOI=10.1128/JB.00124-12;
RA Byrne-Bailey K.G., Coates J.D.;
RT "Complete genome sequence of the anaerobic perchlorate-reducing bacterium
RT Azospira suillum strain PS.";
RL J. Bacteriol. 194:2767-2768(2012).
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=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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003153; AEV24477.1; -; Genomic_DNA.
DR RefSeq; WP_014235179.1; NZ_CAJHOC010000009.1.
DR AlphaFoldDB; G8QLE8; -.
DR STRING; 640081.Dsui_0052; -.
DR KEGG; dsu:Dsui_0052; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_2_4; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000005633; 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:SF125; PYRUVATE KINASE II; 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:AEV24477.1};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 3..323
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 356..469
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 481 AA; 51790 MW; ECE327FCE52CFA76 CRC64;
MARHTKIVAT LGPASTDPVT LERLIRAGVD VVRMNFSHGT AEDHMARART VREISAKVGR
PVGILGDLQG PKIRVGKFEN GKIQLEKGDK FILDANCALG NQERVGLDYK DLPRDVEPGA
VLLLDDGRIV LDVERVIGAE IHTVVRHAGE LSNNKGINRQ GGGLSAPALT AKDMDDIKTA
AQIGVDYIAV SFPKSAADMY MARQLMRAAG SRALTIAKIE RTEAVAALDE ILDASDGVMV
ARGDLAVEVG DAAVPALQKK MIRHAREKNK LAITATQMME SMIQSPVPTR AEVSDVANAV
LDGTDAVMLS AETASGRYPV ETVESMARVC IEAERSAEVT LDREFLDRVF TRIDQSVAMA
AIWTAHHLKV KAIAALSQSG STALWMSRLN CGVPVYALTP DAEAQTKMSL YREVTPLLMS
QQHSDRDVLL YEAEQLLMQN GAVAKGDLIV LTIGEPIGTP GGTNTLKIVR VGEHQMPPLR
A
//
