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Database: UniProt
Entry: A0A093QKQ0_PHACA
LinkDB: A0A093QKQ0_PHACA
Original site: A0A093QKQ0_PHACA 
ID   A0A093QKQ0_PHACA        Unreviewed;       389 AA.
AC   A0A093QKQ0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
DE            EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
DE   Flags: Fragment;
GN   ORFNames=N336_11006 {ECO:0000313|EMBL:KFW89493.1};
OS   Phalacrocorax carbo (Great cormorant) (Pelecanus carbo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Suliformes; Phalacrocoracidae;
OC   Phalacrocorax.
OX   NCBI_TaxID=9209 {ECO:0000313|EMBL:KFW89493.1, ECO:0000313|Proteomes:UP000053238};
RN   [1] {ECO:0000313|EMBL:KFW89493.1, ECO:0000313|Proteomes:UP000053238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N336 {ECO:0000313|EMBL:KFW89493.1};
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=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC         phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC         Evidence={ECO:0000256|RuleBase:RU000532};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5. {ECO:0000256|ARBA:ARBA00004838,
CC       ECO:0000256|RuleBase:RU000532}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245,
CC       ECO:0000256|RuleBase:RU000696}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000256|ARBA:ARBA00008982, ECO:0000256|RuleBase:RU000532}.
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DR   EMBL; KL423102; KFW89493.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093QKQ0; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000053238; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00318; Phosphoglycerate_kinase; 1.
DR   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 3.
DR   HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR   PANTHER; PTHR11406; PHOSPHOGLYCERATE KINASE; 1.
DR   PANTHER; PTHR11406:SF0; PHOSPHOGLYCERATE KINASE; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000724-
KW   2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000532};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053238};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
FT   BINDING         6..8
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         45..48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         202
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         316
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         345..348
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW89493.1"
FT   NON_TER         389
FT                   /evidence="ECO:0000313|EMBL:KFW89493.1"
SQ   SEQUENCE   389 AA;  41742 MW;  81E82DFBCF7C3F97 CRC64;
     VFFRVDFNVP MKDHKITNNQ RIKAAVPTIK HCLDHGAKSV VLMSHLGRPD GVPMPEKFSL
     APVAVELKAL LGREVLFLKD CVGPEVEKAC ANPAAGSVIL LENLRFHVEE EGKGKDASGN
     KIKADPAKVE AFRASLSKLG DVYINDAFGT AHRAHSSMVG VNLPQKAAGF LMKKELDYFA
     KALESPERPF LAILGGAKVQ DKIQLISNML DKVNEMIIGG GMAFTFLKVL NNMEIGNSLF
     DEEGSKIVKD LMAKAEKNGV KITLPVDFVT ADKFDEHAQT GEATGLDCGP ESVKKFVEVV
     GRAKQIVWNG PVGVFEWDKF AKGTKALMDK VVEVTGKGSI TIIGGGDTAT CCAKWNTEDK
     VSHVSTGGGA SLELLEGKVL PGVDALSNV
//
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