ID A0A415DIR6_9BACT Unreviewed; 483 AA.
AC A0A415DIR6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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:RHJ77116.1};
GN ORFNames=DW103_16160 {ECO:0000313|EMBL:RHJ77116.1};
OS Parabacteroides sp. AM08-6.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=2292053 {ECO:0000313|EMBL:RHJ77116.1, ECO:0000313|Proteomes:UP000285678};
RN [1] {ECO:0000313|EMBL:RHJ77116.1, ECO:0000313|Proteomes:UP000285678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM08-6 {ECO:0000313|EMBL:RHJ77116.1,
RC ECO:0000313|Proteomes:UP000285678};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-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=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RHJ77116.1}.
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DR EMBL; QRMP01000037; RHJ77116.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A415DIR6; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000285678; 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; 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; 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.
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:RHJ77116.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000285678};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:RHJ77116.1}.
FT DOMAIN 3..319
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 355..463
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 483 AA; 53741 MW; 90866F293CECB0A9 CRC64;
MLKHTKIVAT VSDQRCDVEF VDALYKAGMN VVRLNTAHMA EEGLSRVVNN VRAVSDRIGI
LMDTKGPEVR TTTAQDAIPF KTGEVVKIMG NPEGETSHEC ICVSYKNFVN DLGIGSDILI
DDGDLELKVI DKKEDYLVCE VQNDSTLGSR KSVNVPGVRI NLPSLTEKDR KNILWAIEND
LDFIAHSFVR NKQDVMDIQR ILDEHNSPIK IIAKIENQEG VDNVDEILEV AYGIMIARGD
LGIEVPAEKI PGIQRVLIRK CVEMKKPVIV ATQMLHSMIN NPRPTRAEVT DIANAIYYRT
DALMLSGETA YGKYPVEAVQ TMTKVAREAE KTKLAANDIR VPIEGNDLDV TSFLAKQAVK
SSSKLHVKAI ITDSYTGRTA RYLAAFRGTS TVFAICYNHR TTRMLSLSYG VWAVYQPFDD
SRRGYFCQAL NELIKSRRIT RNDMVAYLSG SFGEGGGTSF LEINNVGKVL DAGMNYQLPT
FKD
//
