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Database: UniProt
Entry: A0A091UF54_PHALP
LinkDB: A0A091UF54_PHALP
Original site: A0A091UF54_PHALP 
ID   A0A091UF54_PHALP        Unreviewed;       403 AA.
AC   A0A091UF54;
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=N335_11382 {ECO:0000313|EMBL:KFQ72725.1};
OS   Phaethon lepturus (White-tailed tropicbird).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC   Phaethontidae; Phaethon.
OX   NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ72725.1, ECO:0000313|Proteomes:UP000053638};
RN   [1] {ECO:0000313|EMBL:KFQ72725.1, ECO:0000313|Proteomes:UP000053638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ72725.1};
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; KK449536; KFQ72725.1; -; Genomic_DNA.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000053638; 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:UP000053638};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
FT   BINDING         4..6
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         43..46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         299
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         330
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         359..362
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:KFQ72725.1"
FT   NON_TER         403
FT                   /evidence="ECO:0000313|EMBL:KFQ72725.1"
SQ   SEQUENCE   403 AA;  43021 MW;  BADCAECA34E15055 CRC64;
     FRVDFNVPMK DHKITNNQRI KAAVPTIKHC LDHGAKSVVL MSHLGRPDGV PMPEKFSLAP
     VAAELKALMG REVLFLKDCV GPEVEKACAN PAAGSIILLE NLRFHVEEEG KGKDASGNKI
     KADSAKVEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPQKAAGFLM KKELDYFAKA
     LESPERPFLA ILGGAKVQDK IQLISNMLDK VNEMIIGGGM AFTFLKVINN MEIGNSLFDE
     EGSKIVKDLM AKAEKNGVKI TLPVDFITAD KFDEHAQTGE ATVASGTPAX XXXPAGWMGL
     DCGPESVKKF VEVVGRAKQI VWNGPVGVFE WDKFAKGTKA LMDKVVDVTG KGSITIIGGG
     DTATCCAKWN TEDKVSHVST GGGASLELLE GKVLPGVDAL SSV
//
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