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Database: UniProt
Entry: A0A0D1JZI5_9SPHN
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ID   A0A0D1JZI5_9SPHN        Unreviewed;       484 AA.
AC   A0A0D1JZI5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
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=SR41_13640 {ECO:0000313|EMBL:KIU26603.1};
OS   Sphingomonas melonis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=152682 {ECO:0000313|EMBL:KIU26603.1, ECO:0000313|Proteomes:UP000033203};
RN   [1] {ECO:0000313|EMBL:KIU26603.1, ECO:0000313|Proteomes:UP000033203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=30a {ECO:0000313|EMBL:KIU26603.1,
RC   ECO:0000313|Proteomes:UP000033203};
RA   Eevers N., Van Hamme J., Bottos E., Weyens N., Vangronsveld J.;
RT   "Genome of Sphingomonas taxi strain 30a.";
RL   Submitted (JAN-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:KIU26603.1}.
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DR   EMBL; JXTP01000072; KIU26603.1; -; Genomic_DNA.
DR   RefSeq; WP_017980423.1; NZ_QDFS01000001.1.
DR   AlphaFoldDB; A0A0D1JZI5; -.
DR   GeneID; 67492410; -.
DR   PATRIC; fig|1549858.7.peg.3707; -.
DR   OrthoDB; 9812123at2; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000033203; 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:KIU26603.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033203};
KW   Transferase {ECO:0000256|RuleBase:RU000504}.
FT   DOMAIN          10..327
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          360..473
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   484 AA;  52192 MW;  991C086E3EBDD9F0 CRC64;
     MTTAIAPRSR KVRVLATLGP ASNSPEMIAT LFQAGADAFR VNMSHGDQQS KVAVIEAIRA
     LEKEFGRPTT ILADLQGPKL RVGKFDGGRT VLEHNSTFVL DRDPTPGDAT RVELPHKEIF
     EAIEPGARLL LDDGKLVLRV TDHDSDRITT VVEVGGPLSN NKGLNVPDVV LPMAALTEKD
     RSDLAFAVDQ GVDWIALSFV QRPEDLWEAR KLIGGKAALL AKIEKPQAID RLEEIVEACD
     GVMVARGDLG VELPPQSVPP LQKRIVETAR RLGRPVVVAT QMLESMIQSP SPTRAEVSDV
     ATAIYDGADA IMLSAESAAG QWPVESVAMM NSIGVSVESD PMHGDRVHFT VMRPDPTTAD
     ALAEAAKQIA KTVSATAIIC FTTSGSTARR IARERPSVPL LVLTPNRDTA RRLGLLWGTH
     AVHTRDVESF EDMVGKAKRM ALRTGIAHAG DRVIVMAGVP FRTPGSTNVL HVVHITGDEL
     RDYA
//
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