GenomeNet

Database: UniProt
Entry: S5LZ88_9MOLU
LinkDB: S5LZ88_9MOLU
Original site: S5LZ88_9MOLU 
ID   S5LZ88_9MOLU            Unreviewed;       478 AA.
AC   S5LZ88;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
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:AGR41891.1};
GN   ORFNames=SDIMI_v3c01870 {ECO:0000313|EMBL:AGR41891.1};
OS   Spiroplasma diminutum CUAS-1.
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=1276221 {ECO:0000313|EMBL:AGR41891.1, ECO:0000313|Proteomes:UP000014983};
RN   [1] {ECO:0000313|EMBL:AGR41891.1, ECO:0000313|Proteomes:UP000014983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CUAS-1 {ECO:0000313|EMBL:AGR41891.1};
RX   PubMed=23873917; DOI=10.1093/gbe/evt108;
RA   Lo W.S., Ku C., Chen L.L., Chang T.H., Kuo C.H.;
RT   "Comparison of metabolic capacities and inference of gene content evolution
RT   in mosquito-associated Spiroplasma diminutum and S. taiwanense.";
RL   Genome Biol. Evol. 5:1512-1523(2013).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP005076; AGR41891.1; -; Genomic_DNA.
DR   RefSeq; WP_020836124.1; NC_021833.1.
DR   AlphaFoldDB; S5LZ88; -.
DR   STRING; 1276221.SDIMI_v3c01870; -.
DR   KEGG; sdi:SDIMI_v3c01870; -.
DR   PATRIC; fig|1276221.3.peg.184; -.
DR   eggNOG; COG0469; Bacteria.
DR   HOGENOM; CLU_015439_0_2_14; -.
DR   InParanoid; S5LZ88; -.
DR   OrthoDB; 9812123at2; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000014983; 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; 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   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:AGR41891.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014983};
KW   Transferase {ECO:0000256|RuleBase:RU000504}.
FT   DOMAIN          10..336
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
SQ   SEQUENCE   478 AA;  53829 MW;  AD12DC0A850526B5 CRC64;
     MNKFNLTDKM KRTKVITTIG PSVHSKEAIK ELFDKGMTTI RLNFSHADFQ EHGERFEWVK
     ELRKEINKPI SILLDTKGPE IRIGKMKDGK QEVKAGTEIT VYTNPEDFSS RECSATEMQM
     SYDMSQDVKP GDVVLVDDGK LTMHVISVEK FKVMCTAFNT HLVKTNKRVN LPGVEFTLPF
     LAEKDYNDIH FGIESNIDYI AASFVNSADN VNEIRAILKA KNAEHIQIIS KIESQVGCDN
     IDSIIDASDG IMVARGDLGL EIPYYDVPYW EKQIIRKCRE KGKLVIVATQ MLESMTDNPQ
     PTRAEVTDVY YATELGADAT MLSGESANGD FPFITVETMS TINKRAEVEF YEKNYYTKQL
     EKARKSSSGK RAEIANQLAN TTMGGNYEYA IVVSRTGELL RTISKFRPNV TILGVCDNEK
     LWTGFGAMHS IFMSKVEDLD AFMNDDKAIA EIAKSWGAKS GERILFVRNE NIKEITVA
//
DBGET integrated database retrieval system