ID A0A2Z6GFT9_9PROT Unreviewed; 479 AA.
AC A0A2Z6GFT9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=OYT1_ch2612 {ECO:0000313|EMBL:BBE52124.1};
OS Ferriphaselus amnicola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Gallionellaceae; Ferriphaselus.
OX NCBI_TaxID=1188319 {ECO:0000313|EMBL:BBE52124.1, ECO:0000313|Proteomes:UP000033070};
RN [1] {ECO:0000313|EMBL:BBE52124.1, ECO:0000313|Proteomes:UP000033070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OYT1 {ECO:0000313|EMBL:BBE52124.1,
RC ECO:0000313|Proteomes:UP000033070};
RA Kato S., Itoh T., Ohkuma M.;
RT "OYT1 Genome Sequencing.";
RL Submitted (JUN-2018) 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=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}.
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DR EMBL; AP018738; BBE52124.1; -; Genomic_DNA.
DR RefSeq; WP_062626454.1; NZ_AP018738.1.
DR AlphaFoldDB; A0A2Z6GFT9; -.
DR STRING; 1188319.OYT1_01255; -.
DR KEGG; fam:OYT1_ch2612; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000033070; 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:BBE52124.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033070};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 3..324
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 358..470
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 479 AA; 51586 MW; 3BC9A3A287B0AB96 CRC64;
MLRRTKIVAT LGPATSDQKV LEQIIRAGVD VVRMNFSHGT AEDHMGRADR VRAAARAVGR
TVGILADLQG PKIRVRKFEN DKIILNKGDI FILDASWTAL GNQERVGLDY KELPRDVSKG
SVLLLNDGML EFDVEEVRGE EIVCTVVRGG VLSNNKGINR KGGGLTAPAL TDKDKEDIKT
AALIKADFLA VSFPRSADDM KLARELMHAA GGKSLLMAKI ERAEAIPVLS EIIDASDAIM
VARGDLSVEV GDAAVPGLQK RMIKMARAKN KLVITATQMM ESMITNPIPT RAEVSDVANA
VLDGTDAVML SAETAVGDYP VETIQAMARI CIKAEREVED NSMDRRLATQ KFSRIDQSIA
MSALFAASHF KVKAIVALTQ SGSTALWMSR VNAGVPIFAL TPTDATLSKV TLFSGVHPIA
FNPTSVDPAT TLVEAEQELV RLGLVSDDDL MVLTIGDAVG KTGHTNTMRI ARVGDHHKK
//
