PGK_BACAN
ID PGK_BACAN Reviewed; 394 AA.
AC Q81X75; Q6HR11; Q6KKD0;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Phosphoglycerate kinase {ECO:0000255|HAMAP-Rule:MF_00145};
DE EC=2.7.2.3 {ECO:0000255|HAMAP-Rule:MF_00145};
GN Name=pgk {ECO:0000255|HAMAP-Rule:MF_00145};
GN OrderedLocusNames=BA_5367, GBAA_5367, BAS4988;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) 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:0000255|HAMAP-Rule:MF_00145};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5. {ECO:0000255|HAMAP-
CC Rule:MF_00145}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00145}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00145}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00145}.
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DR EMBL; AE016879; AAP29027.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT34502.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT57277.1; -; Genomic_DNA.
DR RefSeq; NP_847541.1; NC_003997.3.
DR RefSeq; WP_001036337.1; NZ_WXXJ01000012.1.
DR RefSeq; YP_031227.1; NC_005945.1.
DR PDB; 3UWD; X-ray; 1.68 A; A=1-394.
DR PDBsum; 3UWD; -.
DR AlphaFoldDB; Q81X75; -.
DR SMR; Q81X75; -.
DR IntAct; Q81X75; 2.
DR STRING; 260799.BAS4988; -.
DR DNASU; 1084905; -.
DR EnsemblBacteria; AAP29027; AAP29027; BA_5367.
DR EnsemblBacteria; AAT34502; AAT34502; GBAA_5367.
DR GeneID; 45024970; -.
DR KEGG; ban:BA_5367; -.
DR KEGG; bar:GBAA_5367; -.
DR KEGG; bat:BAS4988; -.
DR PATRIC; fig|198094.11.peg.5326; -.
DR eggNOG; COG0126; Bacteria.
DR HOGENOM; CLU_025427_0_2_9; -.
DR OMA; DMIFDIG; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
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-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; -; 2.
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; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Glycolysis; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..394
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145899"
FT BINDING 21..23
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 59..62
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 350..353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT MOD_RES 299
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:3UWD"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 41..49
FT /evidence="ECO:0007829|PDB:3UWD"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:3UWD"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:3UWD"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 128..135
FT /evidence="ECO:0007829|PDB:3UWD"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:3UWD"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:3UWD"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 169..183
FT /evidence="ECO:0007829|PDB:3UWD"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:3UWD"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:3UWD"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 243..256
FT /evidence="ECO:0007829|PDB:3UWD"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:3UWD"
FT STRAND 264..271
FT /evidence="ECO:0007829|PDB:3UWD"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:3UWD"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 297..308
FT /evidence="ECO:0007829|PDB:3UWD"
FT STRAND 311..317
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 329..340
FT /evidence="ECO:0007829|PDB:3UWD"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 351..359
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:3UWD"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 374..380
FT /evidence="ECO:0007829|PDB:3UWD"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:3UWD"
SQ SEQUENCE 394 AA; 42298 MW; 0C383DEAA759658A CRC64;
MNKKSIRDVD LKGKRVFCRV DFNVPMKEGK ITDETRIRAA LPTIQYLVEQ GAKVILASHL
GRPKGQAVEE LRLTPVAARL GELLGKDVKK ADEAFGPVAQ EMVAAMNEGD VLVLENVRFY
AGEEKNDAEL AKEFAALADI FVNDAFGAAH RAHASTAGIA DYLPAVSGLL MEKELEVLGK
ALSNPERPFT AIIGGAKVKD KIGLIRHLLD KVDNLIIGGG LAYTFVKALG HEIGLSLCED
DKIELAKEFM QLAKEKGVNF YMPVDVVITE EFSETATTKI VGIDSIPSNW EGVDIGPKTR
EIYADVIKNS KLVVWNGPMG VFEMTPFAEG TKAVGQALAD AEGTYSVIGG GDSAAAVEKF
GMADKMSHIS TGGGASLEFM EGKELPGVVC LNDK
