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Database: UniProt
Entry: A0A158UUE8_RHIBE
LinkDB: A0A158UUE8_RHIBE
Original site: A0A158UUE8_RHIBE 
ID   A0A158UUE8_RHIBE        Unreviewed;       543 AA.
AC   A0A158UUE8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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};
DE   Flags: Fragment;
GN   Name=PKLR {ECO:0000313|Ensembl:ENSRBIP00000028484.1};
OS   Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61621 {ECO:0000313|EMBL:AHW98205.1};
RN   [1] {ECO:0000313|EMBL:AHW98205.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zhang Y.P., Zhou T.C., Shen Y.Y.;
RT   "Natural Selection and Adaptive Evolution of Multiple Genes in Plateau
RT   Indigenous Mammals Driven by the Plateau Environmental Stress.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRBIP00000028484.1, ECO:0000313|Proteomes:UP000233180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu, C.-I. and Zhang, Y.;
RT   "Genome of Rhinopithecus bieti.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSRBIP00000028484.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997,
CC       ECO:0000256|RuleBase:RU000504}.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC       {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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DR   EMBL; KF027427; AHW98205.1; -; mRNA.
DR   Ensembl; ENSRBIT00000052424.1; ENSRBIP00000028484.1; ENSRBIG00000038131.1.
DR   GeneTree; ENSGT00390000008859; -.
DR   OMA; MVRVHHL; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000233180; Unplaced.
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   CDD; cd00288; Pyruvate_Kinase; 1.
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:SF31; PYRUVATE KINASE PKLR; 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   2: Evidence at transcript level;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
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:AHW98205.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW   Transferase {ECO:0000256|RuleBase:RU000504}.
FT   DOMAIN          55..387
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          424..540
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AHW98205.1"
FT   NON_TER         543
FT                   /evidence="ECO:0000313|EMBL:AHW98205.1"
SQ   SEQUENCE   543 AA;  58337 MW;  BF0A07BE85C67BA1 CRC64;
     MEGPAGYLRR ASVAQLTQEL GTAFFQQQQL PAAMADTFLE HLCLLDIDSE PVAARSTSII
     ATIGPASRSV ERLKEMIKAG MNIARLNFSH GSHEYHAESI ANVREAVESF AASPLGYRPV
     AIALDTKGPE IRTGILQGGP ESEVELVKGS QVLVTVDPAF RTRGNANTVW VDYPNVVGVV
     PVGGRIYIDD GLISLVVQKI GPEGLVTQVE NGGVLGSHKG VNLPGAQVDL PGLSEQDVRD
     LRFGVEHGVD IVFASFVRKA SDVAAVRAAL GPEGQGIKII SKIENHEGVK RFDEILEVSD
     GIMVARGDLG IEIPAEKVFL AQKMMIGRCN LAGKPVVCAT QMLESMITKP RPTRAETSDV
     ANAVLDGADC IMLSGETAKG NFPVEAVKMQ HAIAREAEAA VYHRQLFEEL RRAAPLSRDP
     TEVTAIGAVE AAFKCCAAAI IVLTTTGRSA QLLSRYRPRA AVIAVTRSAQ AARQVHLCRG
     VFPLLYREPP EAIWADDVDR RVQFGIESGK LRGFLRVGDL VIVVTGWRPG SGYTNIMRVL
     SIS
//
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