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Database: UniProt
Entry: A0A0R3CWI6_9BRAD
LinkDB: A0A0R3CWI6_9BRAD
Original site: A0A0R3CWI6_9BRAD 
ID   A0A0R3CWI6_9BRAD        Unreviewed;       478 AA.
AC   A0A0R3CWI6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=AOQ71_35640 {ECO:0000313|EMBL:KRQ01939.1};
OS   Bradyrhizobium manausense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=989370 {ECO:0000313|EMBL:KRQ01939.1, ECO:0000313|Proteomes:UP000051936};
RN   [1] {ECO:0000313|EMBL:KRQ01939.1, ECO:0000313|Proteomes:UP000051936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR3351 {ECO:0000313|EMBL:KRQ01939.1,
RC   ECO:0000313|Proteomes:UP000051936};
RA   De Araujo J.L., Zilli J.E.;
RT   "Draft Genome Sequence of Bradyrhizobium manausense Strain BR 3351T, a
RT   Novel Symbiotic Nitrogen-Fixing Alphaproteobacterium Isolated from
RT   Brazilian Amazon Rain Forest.";
RL   Submitted (SEP-2015) 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:KRQ01939.1}.
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DR   EMBL; LJYG01000111; KRQ01939.1; -; Genomic_DNA.
DR   RefSeq; WP_057757285.1; NZ_LJYG01000111.1.
DR   AlphaFoldDB; A0A0R3CWI6; -.
DR   STRING; 989370.AOQ71_35640; -.
DR   OrthoDB; 9812123at2; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000051936; 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:KRQ01939.1};
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   478 AA;  51271 MW;  76503A44CAD70471 CRC64;
     MRRLRRIKIL ATLGPASSDL AMIRRLFEAG ADVFRINMSH TPHDKMRELV ATIRNVESSY
     GRPIGILVDL QGPKLRLGAF AEGAVQLQNG QTFTLDSDKA PGDATRVNLP HPEILAALRP
     GHALLLDDGK VRLIAEETTK EHAVTRVVVG GKMSDRKGVS LPDTDLPVSA MTPKDRADLE
     AALVTGVDWI ALSFVQRADD VIEAKKMIRG RAAVMAKIEK PQAIDRLADI IEASDALMVA
     RGDLGVELPL ERVPSLQKQM TRMARRAGKP VVIATQMLES MIQSPVPTRA EVSDVATAVY
     EGADAIMLSA ESAAGKFPVE AVSTMNRIGE EVERDPTYRS VITAQRPAPE STAGDAIADA
     ARQIAETLDL PALICWTSSG STAVRVARER PKPPIVAITP NITAGRRLAA VWGVHCVVAE
     DARDQDDMVS RAGQIAFRDG FVRAGQRVII VAGVPLGIPG TTNMVRIASV GPEGDANM
//
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