PGK_MYCAV
ID PGK_MYCAV Reviewed; 388 AA.
AC O32848;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
DE Flags: Fragment;
GN Name=pgk;
OS Mycobacterium avium.
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1764;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=101;
RA Parker A.E., Bermudez L.E.;
RT "Mycobacterium avium glyceraldhyde-3-phosphate dehydrogenase homolog.";
RL Submitted (JAN-1998) 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 -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; U82749; AAB95085.1; -; Genomic_DNA.
DR AlphaFoldDB; O32848; -.
DR SMR; O32848; -.
DR UniPathway; UPA00109; UER00185.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 Gene3D; 3.40.50.1260; -; 2.
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; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..>388
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145963"
FT REGION 26..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..136
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 56..59
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 363..366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT NON_TER 388
SQ SEQUENCE 388 AA; 40379 MW; BD5D9478DB686505 CRC64;
MAVHNLKDLL AEGVSGRGVL VRSDLNVPLD SDGEQGRITD PGPDHRVGAD VERTGRGGRQ
GGGRRAPRAS QEWAGPGVVA GPGGRRARRA AGPARAAGLG RGGHRRPGPR RGVDRRRRPA
AGKHPVRRPR NVQGRRRAAR AGRQMAELVG PTGAFVSDGF GVVHRKQASV YDVATLLPHY
AGTLVAEEIA VLEQLTGSTK RPYAVVLGGS KVSDKLGVIE SLATKADSIV IGGGMCFTFL
AAQGFSVGKS LVETEMVDTC RRLLDTYVDV LRLPVDMVAA DRLAADAAPQ TVPADAIPDD
LMGVDIGPGS VKRFTALLSN AETMFWNGPM GVFEFPAFAA GTKGLAEAIA AATGKGAFSV
VGGGDSAAAT AVELQLLFPL VRLIARLA