ID A0A101HMV6_9BACT Unreviewed; 341 AA.
AC A0A101HMV6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Triosephosphate isomerase {ECO:0000256|RuleBase:RU363013};
DE EC=5.3.1.1 {ECO:0000256|RuleBase:RU363013};
DE Flags: Fragment;
GN ORFNames=XD94_1348 {ECO:0000313|EMBL:KUK79558.1};
OS Mesotoga prima.
OC Bacteria; Thermotogota; Thermotogae; Kosmotogales; Kosmotogaceae; Mesotoga.
OX NCBI_TaxID=1184387 {ECO:0000313|EMBL:KUK79558.1, ECO:0000313|Proteomes:UP000054092};
RN [1] {ECO:0000313|Proteomes:UP000054092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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|RuleBase:RU363013};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|RuleBase:RU363013}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate from glycerone phosphate: step 1/1.
CC {ECO:0000256|RuleBase:RU363013}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5. {ECO:0000256|RuleBase:RU000695}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU363013}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000695}.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000256|ARBA:ARBA00007422, ECO:0000256|RuleBase:RU363013}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUK79558.1}.
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DR EMBL; LGGP01000254; KUK79558.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101HMV6; -.
DR PATRIC; fig|1184387.3.peg.1810; -.
DR UniPathway; UPA00109; UER00185.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000054092; Unassembled WGS sequence.
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:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 1.
DR HAMAP; MF_00147_B; TIM_B; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
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; PTHR21139; TRIOSEPHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR21139:SF2; TRIOSEPHOSPHATE ISOMERASE; 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; PS00171; TIM_1; 1.
DR PROSITE; PS51440; TIM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|RuleBase:RU363013};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432,
KW ECO:0000256|RuleBase:RU363013};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000695};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU363013};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KUK79558.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KUK79558.1"
SQ SEQUENCE 341 AA; 36394 MW; 746D1256A09D99D1 CRC64;
KTVVWNGPMG VFEIDDFAKG TESIAKTLAS LKGAVTIIGG GDSAAAINKF GLADRVSHVS
TGGGASLEML EGKEMPGIRS LATKEGKKKR RIMVAGNWKM NKSPNEARMF AGFLASSIGN
EKAVDVVVFP TSLSVAGVAD ILKDTSIKVG VQNIYPADSG AFTGEISVPM LSDLAVEYVL
VGHSERRHIF GETSEMTNEK IKAVLREGLV PIFCVGETLQ ERESGRTEQV LEEQIRKGLA
GLDKSEVEQV IIAYEPVWAI GTGVVATPEQ AEATMKYIRS LLSSLYECSV AERTRILYGG
SIKPDNFDSL IAMENIDGGL VGGASLQESF VQLVAIAKIY A
//
