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Database: UniProt
Entry: A0A1M5J3V3_9ALTE
LinkDB: A0A1M5J3V3_9ALTE
Original site: A0A1M5J3V3_9ALTE 
ID   A0A1M5J3V3_9ALTE        Unreviewed;       478 AA.
AC   A0A1M5J3V3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=SAMN05216361_1930 {ECO:0000313|EMBL:SHG35222.1};
OS   Marisediminitalea aggregata.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Marisediminitalea.
OX   NCBI_TaxID=634436 {ECO:0000313|EMBL:SHG35222.1, ECO:0000313|Proteomes:UP000184520};
RN   [1] {ECO:0000313|Proteomes:UP000184520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.8995 {ECO:0000313|Proteomes:UP000184520};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-2016) 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=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; FQWD01000003; SHG35222.1; -; Genomic_DNA.
DR   RefSeq; WP_073321606.1; NZ_FQWD01000003.1.
DR   AlphaFoldDB; A0A1M5J3V3; -.
DR   STRING; 634436.SAMN05216361_1930; -.
DR   OrthoDB; 9812123at2; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000184520; 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: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:SHG35222.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184520};
KW   Transferase {ECO:0000256|RuleBase:RU000504}.
FT   DOMAIN          3..328
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          360..475
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   478 AA;  50955 MW;  AFA2FD6BA43A5E8E CRC64;
     MTRRTKILAT LGPATDTQEK IEAIIAAGAN VVRMNFSHGQ AEDHIERAKR VRAAARNLGK
     YVAILGDLQG PKIRVSRFEN SAVHLAVGAD FILDAELDRD AGNEKQVGID YKALPDDVSP
     GDILLLDDGR IQLKVTGVEG RKVHTVVTVG GKLSNNKGIN RLGGGLSAEA LTEKDKRDIV
     TAAEIGVDYL AVSFPRSGAD LDYARELAIA AGCNAKICAK VERAEAVATD EAIDDIIRAS
     DAVMVARGDL GVEIGDAELV GVQKKLIARS RQLNKVVITA TQMMESMIDS PMPTRAEVMD
     VANAVLDGTD AVMLSAETAA GNFPVETVQA MARVCEGAET HPSIKFSKHR LDEMFDSVSE
     TIALSAVYAA NHLPGVKAIV GLTESGSTPR LMSRITTKLP IVALSRHEGT LNAMALYRGV
     KPMYFNSSES APGELKNDVV ALLKEHGLVE AGDTFILTHG DRMETIGATN AIKIIDVE
//
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