PGAM1_CHICK
ID PGAM1_CHICK Reviewed; 254 AA.
AC Q5ZLN1; P84174;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Phosphoglycerate mutase 1 {ECO:0000250|UniProtKB:P18669};
DE EC=5.4.2.11 {ECO:0000250|UniProtKB:P18669};
DE EC=5.4.2.4 {ECO:0000250|UniProtKB:P18669};
DE AltName: Full=BPG-dependent PGAM 1;
GN Name=PGAM1 {ECO:0000250|UniProtKB:P18669}; ORFNames=RCJMB04_5g20;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB {ECO:0000312|EMBL:CAG31362.1};
RC TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAG31362.1};
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP IDENTIFICATION, AND MASS SPECTROMETRY.
RC TISSUE=Embryo {ECO:0000269|PubMed:16287166};
RX PubMed=16287166; DOI=10.1002/pmic.200402056;
RA Agudo D., Gomez-Esquer F., Diaz-Gil G., Martinez-Arribas F., Delcan J.,
RA Schneider J., Palomar M.A., Linares R.;
RT "Proteomic analysis of the Gallus gallus embryo at stage-29 of
RT development.";
RL Proteomics 5:4946-4957(2005).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglyceratea crucial step in glycolysis, by using 2,3-
CC bisphosphoglycerate. Also catalyzes the interconversion of (2R)-2,3-
CC bisphosphoglycerate and (2R)-3-phospho-glyceroyl phosphate.
CC {ECO:0000250|UniProtKB:P18669}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000250|UniProtKB:P18669};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15903;
CC Evidence={ECO:0000250|UniProtKB:P18669};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-
CC bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58248; EC=5.4.2.4;
CC Evidence={ECO:0000250|UniProtKB:P18669};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P18669}.
CC -!- MASS SPECTROMETRY: Mass=28769; Mass_error=1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16287166};
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000255}.
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DR EMBL; AJ719703; CAG31362.1; -; mRNA.
DR RefSeq; NP_001026727.1; NM_001031556.2.
DR AlphaFoldDB; Q5ZLN1; -.
DR SMR; Q5ZLN1; -.
DR BioGRID; 687887; 2.
DR IntAct; Q5ZLN1; 1.
DR STRING; 9031.ENSGALP00000038677; -.
DR PaxDb; Q5ZLN1; -.
DR PRIDE; Q5ZLN1; -.
DR Ensembl; ENSGALT00000039466; ENSGALP00000038677; ENSGALG00000007606.
DR GeneID; 428969; -.
DR KEGG; gga:428969; -.
DR CTD; 5223; -.
DR VEuPathDB; HostDB:geneid_428969; -.
DR eggNOG; KOG0235; Eukaryota.
DR GeneTree; ENSGT00950000182926; -.
DR HOGENOM; CLU_033323_1_1_1; -.
DR InParanoid; Q5ZLN1; -.
DR OMA; RMLPYWY; -.
DR OrthoDB; 804949at2759; -.
DR PhylomeDB; Q5ZLN1; -.
DR Reactome; R-GGA-352875; Gluconeogenesis.
DR Reactome; R-GGA-352882; Glycolysis.
DR SABIO-RK; Q5ZLN1; -.
DR PRO; PR:Q5ZLN1; -.
DR Proteomes; UP000000539; Chromosome 6.
DR Bgee; ENSGALG00000007606; Expressed in muscle tissue and 13 other tissues.
DR ExpressionAtlas; Q5ZLN1; baseline and differential.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; ISS:UniProtKB.
DR GO; GO:0004082; F:bisphosphoglycerate mutase activity; ISS:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; TAS:Reactome.
DR GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
DR GO; GO:0006096; P:glycolytic process; TAS:Reactome.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR PANTHER; PTHR11931; PTHR11931; 1.
DR Pfam; PF00300; His_Phos_1; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR TIGRFAMs; TIGR01258; pgm_1; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Glycolysis; Hydrolase; Isomerase; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..254
FT /note="Phosphoglycerate mutase 1"
FT /id="PRO_0000223502"
FT ACT_SITE 11
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT BINDING 10..17
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 23..24
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 89..92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 187..188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT SITE 186
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250"
FT MOD_RES 26
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 254 AA; 28898 MW; E96705B2E5F7F227 CRC64;
MAAYRLVLVR HGESAWNLEN RFCGWYDADL SPAGQQEARR GGEALRDAGY EFDICFTSVQ
KRAIRTLWNV LDAIDQMWLP VVRTWRLNER HYGALTGLNK AETAAKHGEA QVKIWRRSFD
IPPPPMQSDH PFFSTISKDR RYADLTEDQL PTCESLKDTI ARALPFWNEE IVPQIKEGKR
VLIAAHGNSL RGIVKHLEGM SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVR
KAMEAVAAQG KVKK
