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Database: UniProt
Entry: A0A194QMB2_PAPMA
LinkDB: A0A194QMB2_PAPMA
Original site: A0A194QMB2_PAPMA 
ID   A0A194QMB2_PAPMA        Unreviewed;       415 AA.
AC   A0A194QMB2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   28-JUN-2023, entry version 29.
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};
GN   ORFNames=RR48_11714 {ECO:0000313|EMBL:KPJ06667.1};
OS   Papilio machaon (Old World swallowtail butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Papilionidae; Papilioninae; Papilio.
OX   NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ06667.1, ECO:0000313|Proteomes:UP000053240};
RN   [1] {ECO:0000313|EMBL:KPJ06667.1, ECO:0000313|Proteomes:UP000053240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ06667.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KPJ06667.1};
RX   PubMed=26354079; DOI=10.1038/ncomms9212;
RA   Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA   Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA   Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA   Wang W.;
RT   "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL   Nat. Commun. 6:8212-8212(2015).
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; KQ461195; KPJ06667.1; -; Genomic_DNA.
DR   RefSeq; XP_014369493.1; XM_014514007.1.
DR   AlphaFoldDB; A0A194QMB2; -.
DR   STRING; 76193.A0A194QMB2; -.
DR   GeneID; 106719632; -.
DR   KEGG; pmac:106719632; -.
DR   InParanoid; A0A194QMB2; -.
DR   OrthoDB; 5477183at2759; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000053240; 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; IPR015911; Phosphoglycerate_kinase_CS.
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.
DR   PROSITE; PS00111; PGLYCERATE_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:UP000053240};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
FT   BINDING         23..25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         62..65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         218
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         311
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         371..374
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
SQ   SEQUENCE   415 AA;  44154 MW;  B73A2DFA4AE0370A CRC64;
     MALNKLSIDA LNLAGKRVLM RVDFNVPLKD GVITNNQRIV AALDSVKFAL DKGAKSVVLM
     SHLGRPDGQA NLKYTLKPVA DELKKLLNKD VTFLKDCVGS EVEAACADPP TGSIILLENL
     RFHIEEEGKG VDASGAKVKA DAEKVKAFRA SLRKLGDVYI NDAFGTAHRA HSSMMGEGFE
     QRASGFLLKK ELQYFAKALH EPERPFLAIL GGAKVADKIL LIENLLDKVN EMIIGGGMAY
     TFLKETKGMS IGNSLYDGEG AKIVGKLLEK AAKNNVKVHL PVDFITADKF DENAQVGTAD
     VDSGIPDGWM GLDVGPKTRE LFADPIARAK VIVWNGPAGV FEFEKFAGGT RALMDCVVKA
     TNNGAVTIIG GGDTATCCAK WGTEDKVSHV STGGGASLEL LEGKVLPGVA ALSDA
//
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