ID A0LTX7_ACIC1 Unreviewed; 687 AA.
AC A0LTX7;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00145, ECO:0000256|HAMAP-Rule:MF_00147};
DE Includes:
DE RecName: Full=Triosephosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147};
DE Short=TIM {ECO:0000256|HAMAP-Rule:MF_00147};
DE Short=TPI {ECO:0000256|HAMAP-Rule:MF_00147};
DE EC=5.3.1.1 {ECO:0000256|HAMAP-Rule:MF_00147};
DE AltName: Full=Triose-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147};
DE Includes:
DE RecName: Full=Phosphoglycerate kinase {ECO:0000256|HAMAP-Rule:MF_00145};
DE EC=2.7.2.3 {ECO:0000256|HAMAP-Rule:MF_00145};
GN Name=pgk {ECO:0000256|HAMAP-Rule:MF_00145};
GN Synonyms=tpiA {ECO:0000256|HAMAP-Rule:MF_00147};
GN OrderedLocusNames=Acel_1115 {ECO:0000313|EMBL:ABK52887.1};
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC Acidothermus.
OX NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK52887.1, ECO:0000313|Proteomes:UP000008221};
RN [1] {ECO:0000313|EMBL:ABK52887.1, ECO:0000313|Proteomes:UP000008221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B
RC {ECO:0000313|Proteomes:UP000008221};
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(2009).
CC -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically
CC the conversion of dihydroxyacetone phosphate (DHAP) to D-
CC glyceraldehyde-3-phosphate (G3P). {ECO:0000256|HAMAP-Rule:MF_00147}.
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|ARBA:ARBA00000642, ECO:0000256|HAMAP-
CC Rule:MF_00145};
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; Evidence={ECO:0000256|HAMAP-Rule:MF_00147};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|HAMAP-Rule:MF_00147}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate from glycerone phosphate: step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_00147}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5. {ECO:0000256|HAMAP-
CC Rule:MF_00145}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00147}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00145}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000256|HAMAP-Rule:MF_00145}.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000256|HAMAP-Rule:MF_00147}.
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DR EMBL; CP000481; ABK52887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0LTX7; -.
DR STRING; 351607.Acel_1115; -.
DR KEGG; ace:Acel_1115; -.
DR eggNOG; COG0126; Bacteria.
DR eggNOG; COG0149; Bacteria.
DR HOGENOM; CLU_025427_3_3_11; -.
DR InParanoid; A0LTX7; -.
DR OrthoDB; 9808460at2; -.
DR UniPathway; UPA00109; UER00185.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000008221; 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:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR CDD; cd00311; TIM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 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 NCBIfam; TIGR00419; tim; 1.
DR PANTHER; PTHR11406; PHOSPHOGLYCERATE KINASE; 1.
DR PANTHER; PTHR11406:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00162; PGK; 1.
DR Pfam; PF00121; TIM; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR SUPFAM; SSF51351; Triosephosphate isomerase (TIM); 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
DR PROSITE; PS00171; TIM_1; 1.
DR PROSITE; PS51440; TIM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00145}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP-
KW Rule:MF_00147};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_00145};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00147};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00145};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00145}; Reference proteome {ECO:0000313|Proteomes:UP000008221};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00145}.
FT REGION 411..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 530
FT /note="Electrophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
FT ACT_SITE 602
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
FT BINDING 19..21
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145"
FT BINDING 61..64
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145"
FT BINDING 306
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145"
FT BINDING 337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145"
FT BINDING 363..366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145"
FT BINDING 440..442
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
FT BINDING 608
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
FT BINDING 648
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
FT BINDING 669..670
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
SQ SEQUENCE 687 AA; 72734 MW; D6F4C9E0030012D0 CRC64;
MRSVDDLEVA GRTVFVRVDL NVPLEATDQG PRITDDKRIQ ASLPTIRDLL GRGARVVLLA
HLGRPKGEVR PELSLRPVAA RLAELLGEPV AFPDTTDGGV AGEAARALVA QLRPGQAALL
ENLRFEAAET SKDDAERAAF AERLIALAGE EGALYVGDGF GAVHRKHASV YDLPLRLPHA
AGRLVLAEVS VLRRLTENPD RPYVVVLGGA KVSDKLGVIA NLLEKVDRLL IGGGMAYTFL
AAQGHEVGRS ILEADQVDAV RGFLAEAEKR GVDLVLPVDI VAASHYAPDA DHVVVPATAI
PADREGLDIG PQTRELFAAK LADARTVFWN GPMGVFEFDA FAAGTRAVAE AIARLDGLTV
IGGGDSAAAV RKLGFPESAF RHVSTGGGAS LEYLEGKELP GLQALEADTR QGTAGPSGVG
GRHAVSRSGS PARKPLMAGN WKMHYTHLEA IAHVQKLAFI LSEADYERVE VAVLPPFTAI
RSVQTLVDGD KLPIRYGAQD VSPYPSGAYT GDISAGMLAK LGCSYVIVGH SERRHYHHEN
DELINAKVRA VIGAEMTPIL CVGEPLDVRR SGRHVEFTLG QLDADLAGLS AEQVASLVIA
YEPVWAIGTG EVATPKDAQE VCAAIRARLA ESFGDAAARS ARILYGGSVK SDNAGGIMEE
PDVDGALVGG ASLDAEEFAR IVRYDTK
//
