ID A0A2T6F1V0_9BURK Unreviewed; 473 AA.
AC A0A2T6F1V0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:PUA17025.1};
GN ORFNames=C7W93_13760 {ECO:0000313|EMBL:PUA17025.1};
OS Glaciimonas sp. PCH181.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Glaciimonas.
OX NCBI_TaxID=2133943 {ECO:0000313|EMBL:PUA17025.1, ECO:0000313|Proteomes:UP000244112};
RN [1] {ECO:0000313|EMBL:PUA17025.1, ECO:0000313|Proteomes:UP000244112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCH181 {ECO:0000313|EMBL:PUA17025.1,
RC ECO:0000313|Proteomes:UP000244112};
RA Kumar V., Thakur V., Kumar S., Singh D.;
RT "Genome analysis of a novel bacterium Glaciimonas sp. PCH181 isolated from
RT glacier stream of Indian trans-Himalaya.";
RL Submitted (MAR-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 -!- 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:PUA17025.1}.
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DR EMBL; PYFP01000002; PUA17025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6F1V0; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000244112; 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:PUA17025.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244112};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 5..322
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 355..467
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 473 AA; 51530 MW; 1E197BF68AE927A8 CRC64;
MRRQRNAKIV ATLGPTSSSQ EMIQTLFEAG ADVFRFNFSH GSHADHQERH RIVREIERLV
GRPIAILADL QGPKLRIGQF AEGKVTLHAG QEFVLDRDTS LGNTQRVCLP HPELFAVITA
GQSLLLDDGK LRLQVQDSDG QRIRTRVVNG GVLSDRKGVN VPDAVLPIPA LTEKDKRDLA
FALELGVDWV ALSFVQRPED VLEAKALIGD RAWVLSKLEK PAALDQLDAI VQASDAIMVA
RGDLGVELPP ERVPGVQKRI LRVCRQHGKP IVIATQMLES MITMPVPTRA EASDVASAIY
DGSDAVMLSA ESASGAYPVE AVEMMSRIIA EVEQDPLYRN MLDAQHQTPL PNRGDAICSA
LRDVTRIVGA KATVTYTSSG HTSLRAARER PIAPIVSITP KLATARRLAM VWGVHSTISD
QVHNESEMVK AACETAFKEG FAEIGDQIAI TAGMPFGEPG STNLLRLAEI WPQ
//
