(data stored in ACNUC7421 zone)

SWISSPROT: D6ZCQ8_SEGRD

ID   D6ZCQ8_SEGRD            Unreviewed;       264 AA.
AC   D6ZCQ8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   RecName: Full=Triosephosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728730};
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, ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728682};
DE   AltName: Full=Triose-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147};
GN   Name=tpiA {ECO:0000256|HAMAP-Rule:MF_00147};
GN   OrderedLocusNames=Srot_0618 {ECO:0000313|EMBL:ADG97100.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG97100.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG97100.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
CC   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes
CC       stereospecifically the conversion of dihydroxyacetone phosphate
CC       (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000256|HAMAP-
CC       Rule:MF_00147}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone
CC         phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00147, ECO:0000256|RuleBase:RU363013,
CC         ECO:0000256|SAAS:SAAS01116239};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013,
CC       ECO:0000256|SAAS:SAAS00728615}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_00147, ECO:0000256|RuleBase:RU363013,
CC       ECO:0000256|SAAS:SAAS00728661}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00147,
CC       ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728692}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00147,
CC       ECO:0000256|RuleBase:RU363013}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013,
CC       ECO:0000256|SAAS:SAAS00728708}.
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DR   EMBL; CP001958; ADG97100.1; -; Genomic_DNA.
DR   RefSeq; WP_013137556.1; NC_014168.1.
DR   STRING; 640132.Srot_0618; -.
DR   EnsemblBacteria; ADG97100; ADG97100; Srot_0618.
DR   KEGG; srt:Srot_0618; -.
DR   eggNOG; ENOG4105CP7; Bacteria.
DR   eggNOG; COG0149; LUCA.
DR   HOGENOM; HOG000226414; -.
DR   KO; K01803; -.
DR   OMA; LCVGEGL; -.
DR   OrthoDB; 1266295at2; -.
DR   BioCyc; SROT640132:G1GLH-623-MONOMER; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000002247; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   CDD; cd00311; TIM; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00147_B; TIM_B; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
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; PTHR21139; PTHR21139; 1.
DR   Pfam; PF00121; TIM; 1.
DR   SUPFAM; SSF51351; SSF51351; 1.
DR   TIGRFAMs; TIGR00419; tim; 1.
DR   PROSITE; PS00171; TIM_1; 1.
DR   PROSITE; PS51440; TIM_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6ZCQ8.
DR   SWISS-2DPAGE; D6ZCQ8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00147,
KW   ECO:0000256|RuleBase:RU363013};
KW   Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00147,
KW   ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728593};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_00147,
KW   ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728672};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00147,
KW   ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00498630,
KW   ECO:0000313|EMBL:ADG97100.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247}.
FT   REGION       13     15       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00147}.
FT   REGION      242    243       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00147}.
FT   ACT_SITE    103    103       Electrophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00147}.
FT   ACT_SITE    175    175       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00147}.
FT   BINDING     181    181       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00147}.
FT   BINDING     221    221       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00147}.
SQ   SEQUENCE   264 AA;  27707 MW;  829F7E8238CE5480 CRC64;
     MTSPSRQPLI AGNWKMNLNH FEAIALVQKL CHALKAEHFE TVQTSVLVPF TDIRSVQAVV
     ESDGLPVEYG AQDLSKHDAG AYTGEVSGAF LAKLGCTQVV VGHSERRAYH HETDELVAAK
     AKAALKHGLT PIVCVGEGED VREAGRHIAH CDSQLRASLA GLSEDELAKV VIAYEPVWAI
     GTGRVASPKD AQEVCGAMRK ALAEIGGDHV ARAARVLYGG SVNKGNAAEL LAEPDVDGAL
     VGGASLKVEE FAAIVAFAAL AAKS
//

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