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Database: UniProt
Entry: D3RML8_ALLVD
LinkDB: D3RML8_ALLVD
Original site: D3RML8_ALLVD 
ID   D3RML8_ALLVD            Unreviewed;       480 AA.
AC   D3RML8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 72.
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   OrderedLocusNames=Alvin_0313 {ECO:0000313|EMBL:ADC61276.1};
OS   Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS   10441 / D) (Chromatium vinosum).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Allochromatium.
OX   NCBI_TaxID=572477 {ECO:0000313|EMBL:ADC61276.1, ECO:0000313|Proteomes:UP000001441};
RN   [1] {ECO:0000313|EMBL:ADC61276.1, ECO:0000313|Proteomes:UP000001441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D
RC   {ECO:0000313|Proteomes:UP000001441};
RX   PubMed=22675582; DOI=10.4056/sigs.2335270;
RA   Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA   Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT   "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL   Stand. Genomic Sci. 5:311-330(2011).
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=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}.
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DR   EMBL; CP001896; ADC61276.1; -; Genomic_DNA.
DR   RefSeq; WP_012969552.1; NC_013851.1.
DR   AlphaFoldDB; D3RML8; -.
DR   STRING; 572477.Alvin_0313; -.
DR   KEGG; alv:Alvin_0313; -.
DR   eggNOG; COG0469; Bacteria.
DR   HOGENOM; CLU_015439_0_2_6; -.
DR   OMA; RVHHIGE; -.
DR   OrthoDB; 9812123at2; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000001441; 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; 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:SF125; PYRUVATE KINASE II; 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:ADC61276.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001441};
KW   Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:ADC61276.1}.
FT   DOMAIN          3..325
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          355..469
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   480 AA;  51906 MW;  87536021110B13AF CRC64;
     MPRRTKIVAT LGPATDPVSV TDEILAAGVD VVRLNLSHDT HDRHRERAAR IRERALAAGQ
     EIAVLMDLQG PKIRIGKFTD GKIQLARGDR FAIDTHCPID AGDRTRVGTT YVELANDVRH
     GDTLLLDDGA IELWVDAVVD GRIACQVVTG GTLSNNKGIN KKGGGLSAPA LTDKDKDDIR
     FAAEIDADYL AVSFVRNGDD VRLARELFYE AGGRGGIVAK IERAESLKGI DDIINAADAI
     MVARGDLGVE IGDAELPAVQ KRLISRAREL NSVVITATQM MQSMIESPIP TRAEVFDVAN
     AVLDGTDAVM LSAESSIGKN PAKVVEALDR ICLEAEKSAT RSGHRLDSVF GRVDEAIAMA
     AMYTANHLGV KAIAALTETG STVKWMSRIS SGIPIYGLTR SVPTQRKVRL FRGVYPVAFD
     VASTDMHEVN REVIEELLRH GTVQHGDLVI ITKGDRSGVE GQTNIMKIMR VGEHRLLNED
//
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