PGKT_THEMA
ID PGKT_THEMA Reviewed; 654 AA.
AC P36204; Q60031;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 4.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Bifunctional PGK/TIM;
DE Includes:
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
DE Includes:
DE RecName: Full=Triosephosphate isomerase;
DE Short=TIM;
DE EC=5.3.1.1;
DE AltName: Full=Triose-phosphate isomerase;
GN Name=pgk/tpi; OrderedLocusNames=TM_0689;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=7859734; DOI=10.1002/j.1460-2075.1995.tb07020.x;
RA Schurig H., Beaucamp N., Ostendorp R., Jaenicke R., Adler E., Knowles J.R.;
RT "Phosphoglycerate kinase and triosephosphate isomerase from the
RT hyperthermophilic bacterium Thermotoga maritima form a covalent
RT bifunctional enzyme complex.";
RL EMBO J. 14:442-451(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-393 IN COMPLEX WITH SUBSTRATE
RP AND ATP ANALOG, AND SEQUENCE REVISION.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=9384563; DOI=10.1016/s0969-2126(97)00297-9;
RA Auerbach G., Huber R., Graettinger M., Zaiss K., Schurig H., Jaenicke R.,
RA Jacob U.;
RT "Closed structure of phosphoglycerate kinase from Thermotoga maritima
RT reveals the catalytic mechanism and determinants of thermal stability.";
RL Structure 5:1475-1483(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 400-654, AND SUBUNIT.
RX PubMed=10591103;
RX DOI=10.1002/(sici)1097-0134(19991115)37:3<441::aid-prot11>3.0.co;2-7;
RA Maes D., Zeelen J.P., Thanki N., Beaucamp N., Alvarez M., Thi M.H.,
RA Backmann J., Martial J.A., Wyns L., Jaenicke R., Wierenga R.K.;
RT "The crystal structure of triosephosphate isomerase (TIM) from Thermotoga
RT maritima: a comparative thermostability structural analysis of ten
RT different TIM structures.";
RL Proteins 37:441-453(1999).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate;
CC Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776;
CC EC=5.3.1.1;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate from glycerone phosphate: step 1/1.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer (PGK) and homotetramer (PGK-TIM).
CC {ECO:0000269|PubMed:10591103, ECO:0000269|PubMed:7859734,
CC ECO:0000269|PubMed:9384563}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: In the N-terminal section; belongs to the phosphoglycerate
CC kinase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the triosephosphate
CC isomerase family. {ECO:0000305}.
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DR EMBL; X75437; CAA53187.1; -; Genomic_DNA.
DR EMBL; L27492; AAA67520.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD35771.1; -; Genomic_DNA.
DR PIR; G72344; G72344.
DR RefSeq; NP_228498.1; NC_000853.1.
DR RefSeq; WP_004081072.1; NZ_CP011107.1.
DR PDB; 1B9B; X-ray; 2.85 A; A/B=400-654.
DR PDB; 1VPE; X-ray; 2.00 A; A=2-398.
DR PDBsum; 1B9B; -.
DR PDBsum; 1VPE; -.
DR AlphaFoldDB; P36204; -.
DR SMR; P36204; -.
DR STRING; 243274.THEMA_01220; -.
DR DrugBank; DB04510; 3-phospho-D-glyceric acid.
DR EnsemblBacteria; AAD35771; AAD35771; TM_0689.
DR KEGG; tma:TM0689; -.
DR eggNOG; COG0126; Bacteria.
DR eggNOG; COG0149; Bacteria.
DR InParanoid; P36204; -.
DR OMA; FYKNEGA; -.
DR OrthoDB; 90424at2; -.
DR BioCyc; MetaCyc:MON-382; -.
DR BRENDA; 5.3.1.1; 6331.
DR SABIO-RK; P36204; -.
DR UniPathway; UPA00109; UER00185.
DR UniPathway; UPA00109; UER00189.
DR EvolutionaryTrace; P36204; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IBA:GO_Central.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR CDD; cd00311; TIM; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.50.1260; -; 2.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR HAMAP; MF_00147_B; TIM_B; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR InterPro; IPR035990; TIM_sf.
DR InterPro; IPR022896; TrioseP_Isoase_bac/euk.
DR InterPro; IPR000652; Triosephosphate_isomerase.
DR InterPro; IPR020861; Triosephosphate_isomerase_AS.
DR PANTHER; PTHR11406; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR Pfam; PF00121; TIM; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF51351; SSF51351; 1.
DR SUPFAM; SSF53748; SSF53748; 1.
DR TIGRFAMs; TIGR00419; tim; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
DR PROSITE; PS00171; TIM_1; 1.
DR PROSITE; PS51440; TIM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Fatty acid biosynthesis;
KW Fatty acid metabolism; Gluconeogenesis; Glycolysis; Isomerase; Kinase;
KW Lipid biosynthesis; Lipid metabolism; Multifunctional enzyme;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..654
FT /note="Bifunctional PGK/TIM"
FT /id="PRO_0000146025"
FT REGION 1..399
FT /note="Phosphoglycerate kinase"
FT REGION 400..654
FT /note="Triosephosphate isomerase"
FT ACT_SITE 495
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 567
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 21..23
FT /ligand="substrate"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9384563"
FT BINDING 59..62
FT /ligand="substrate"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9384563"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9384563"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 324
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 353..356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 409..411
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 572
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 634..635
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT CONFLICT 213
FT /note="D -> N (in Ref. 1; CAA53187)"
FT /evidence="ECO:0000305"
FT CONFLICT 394..396
FT /note="IAD -> MRI (in Ref. 1; CAA53187)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="K -> R (in Ref. 1; CAA53187)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="E -> Q (in Ref. 1; CAA53187)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:1VPE"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:1VPE"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:1VPE"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:1VPE"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1VPE"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:1VPE"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 128..135
FT /evidence="ECO:0007829|PDB:1VPE"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1VPE"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:1VPE"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 169..183
FT /evidence="ECO:0007829|PDB:1VPE"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:1VPE"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:1VPE"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:1VPE"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:1VPE"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:1VPE"
FT STRAND 264..271
FT /evidence="ECO:0007829|PDB:1VPE"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:1VPE"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:1VPE"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 298..308
FT /evidence="ECO:0007829|PDB:1VPE"
FT STRAND 312..318
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 330..344
FT /evidence="ECO:0007829|PDB:1VPE"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 354..362
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:1VPE"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 376..383
FT /evidence="ECO:0007829|PDB:1VPE"
FT HELIX 389..392
FT /evidence="ECO:0007829|PDB:1VPE"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:1B9B"
FT HELIX 416..429
FT /evidence="ECO:0007829|PDB:1B9B"
FT STRAND 435..441
FT /evidence="ECO:0007829|PDB:1B9B"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:1B9B"
FT HELIX 447..454
FT /evidence="ECO:0007829|PDB:1B9B"
FT STRAND 457..464
FT /evidence="ECO:0007829|PDB:1B9B"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:1B9B"
FT HELIX 480..484
FT /evidence="ECO:0007829|PDB:1B9B"
FT TURN 485..487
FT /evidence="ECO:0007829|PDB:1B9B"
FT STRAND 490..494
FT /evidence="ECO:0007829|PDB:1B9B"
FT HELIX 496..500
FT /evidence="ECO:0007829|PDB:1B9B"
FT HELIX 506..518
FT /evidence="ECO:0007829|PDB:1B9B"
FT STRAND 522..527
FT /evidence="ECO:0007829|PDB:1B9B"
FT HELIX 531..536
FT /evidence="ECO:0007829|PDB:1B9B"
FT HELIX 539..551
FT /evidence="ECO:0007829|PDB:1B9B"
FT HELIX 556..559
FT /evidence="ECO:0007829|PDB:1B9B"
FT STRAND 563..566
FT /evidence="ECO:0007829|PDB:1B9B"
FT HELIX 569..571
FT /evidence="ECO:0007829|PDB:1B9B"
FT STRAND 572..575
FT /evidence="ECO:0007829|PDB:1B9B"
FT HELIX 580..597
FT /evidence="ECO:0007829|PDB:1B9B"
FT HELIX 600..605
FT /evidence="ECO:0007829|PDB:1B9B"
FT STRAND 606..613
FT /evidence="ECO:0007829|PDB:1B9B"
FT HELIX 616..619
FT /evidence="ECO:0007829|PDB:1B9B"
FT TURN 620..622
FT /evidence="ECO:0007829|PDB:1B9B"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:1B9B"
FT STRAND 630..634
FT /evidence="ECO:0007829|PDB:1B9B"
FT HELIX 635..637
FT /evidence="ECO:0007829|PDB:1B9B"
FT HELIX 641..649
FT /evidence="ECO:0007829|PDB:1B9B"
SQ SEQUENCE 654 AA; 71585 MW; 42358A4EF0C5E481 CRC64;
MEKMTIRDVD LKGKRVIMRV DFNVPVKDGV VQDDTRIRAA LPTIKYALEQ GAKVILLSHL
GRPKGEPSPE FSLAPVAKRL SELLGKEVKF VPAVVGDEVK KAVEELKEGE VLLLENTRFH
PGETKNDPEL AKFWASLADI HVNDAFGTAH RAHASNVGIA QFIPSVAGFL MEKEIKFLSK
VTYNPEKPYV VVLGGAKVSD KIGVITNLME KADRILIGGA MMFTFLKALG KEVGSSRVEE
DKIDLAKELL EKAKEKGVEI VLPVDAVIAQ KIEPGVEKKV VRIDDGIPEG WMGLDIGPET
IELFKQKLSD AKTVVWNGPM GVFEIDDFAE GTKQVALAIA ALTEKGAITV VGGGDSAAAV
NKFGLEDKFS HVSTGGGASL EFLEGKELPG IASIADKKKI TRKLILAGNW KMHKTISEAK
KFVSLLVNEL HDVKEFEIVV CPPFTALSEV GEILSGRNIK LGAQNVFYED QGAFTGEISP
LMLQEIGVEY VIVGHSERRR IFKEDDEFIN RKVKAVLEKG MTPILCVGET LEEREKGLTF
CVVEKQVREG FYGLDKEEAK RVVIAYEPVW AIGTGRVATP QQAQEVHAFI RKLLSEMYDE
ETAGSIRILY GGSIKPDNFL GLIVQKDIDG GLVGGASLKE SFIELARIMR GVIS
