ID A0A091SIA0_PELCR Unreviewed; 532 AA.
AC A0A091SIA0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Pyruvate kinase {ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|RuleBase:RU000504};
DE Flags: Fragment;
GN ORFNames=N334_11089 {ECO:0000313|EMBL:KFQ58349.1};
OS Pelecanus crispus (Dalmatian pelican).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Pelecanidae; Pelecanus.
OX NCBI_TaxID=36300 {ECO:0000313|EMBL:KFQ58349.1, ECO:0000313|Proteomes:UP000054150};
RN [1] {ECO:0000313|EMBL:KFQ58349.1, ECO:0000313|Proteomes:UP000054150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N334 {ECO:0000313|EMBL:KFQ58349.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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 -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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DR EMBL; KK473817; KFQ58349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091SIA0; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000054150; 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 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; 2.
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:SF101; PYRUVATE KINASE PKM; 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:KFQ58349.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054150};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 44..376
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 411..529
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ58349.1"
FT NON_TER 532
FT /evidence="ECO:0000313|EMBL:KFQ58349.1"
SQ SEQUENCE 532 AA; 58159 MW; A2C059A6D4ABE325 CRC64;
ATMSKHHDAG TAFIQTQQLH AAMADTFLEH MCRLDIDSEP TIARNTGIIC TIGPASRSVE
KLKEMIKSGM NVARLNFSHG THEYHEGTIK NVREATESFA SDPITYRPVA IALDTKGPEI
RTGLIKGSGT AEVELKKGAP LKVTLDDAFM EKCDENMLWV DYKNLTKVVE VGSKIYVDDG
LISLLVKEKG KDYVMTEIEN GGMLGSKKGV NLPGAAVDLP AVSEKDIQDL KFGVEQNVDM
VFASFIRKAA DVHAVRKVLG EKGKNIKIIS KIENHEGVRR FDEIMEASDG IMVARGDLGI
EIPAEKVFLA QKMMIGRCNR AGKPIICATQ MLESMIKKPR PTRAEGSDVA NAVLDGADCI
MLSGETAKGD YPLEAVRMQH AIAREAEAAI FHRQLFEELR RLTSLNCDPT EAAAVGAVEA
SFKCCSGAII VLTKSGRSAH LVSRYRPRAP IIAVTRNDQT ARQAHLYRGI FPVLCKEPAH
DSWAEDVDLR VNLGMNVGKA RGFFKTGDLV IVLTGWRPGS GYTNTMRVVP VP
//
