(data stored in SCRATCH zone)

SWISSPROT: C3MIA6_SINFN

ID   C3MIA6_SINFN            Unreviewed;       261 AA.
AC   C3MIA6;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 61.
DE   RecName: Full=Triosephosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013};
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};
DE   AltName: Full=Triose-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147};
GN   Name=tpiA {ECO:0000256|HAMAP-Rule:MF_00147,
GN   ECO:0000313|EMBL:ACP24454.1};
GN   OrderedLocusNames=NGR_c06610 {ECO:0000313|EMBL:ACP24454.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24454.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24454.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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: D-glyceraldehyde 3-phosphate = glycerone
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_00147,
CC       ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728719}.
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00147}.
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DR   EMBL; CP001389; ACP24454.1; -; Genomic_DNA.
DR   RefSeq; WP_012707239.1; NC_012587.1.
DR   RefSeq; YP_002825207.1; NC_012587.1.
DR   ProteinModelPortal; C3MIA6; -.
DR   STRING; 394.NGR_c06610; -.
DR   EnsemblBacteria; ACP24454; ACP24454; NGR_c06610.
DR   GeneID; 7791887; -.
DR   KEGG; rhi:NGR_c06610; -.
DR   PATRIC; fig|394.7.peg.3474; -.
DR   eggNOG; ENOG4105CP7; Bacteria.
DR   eggNOG; COG0149; LUCA.
DR   HOGENOM; HOG000226412; -.
DR   KO; K01803; -.
DR   OMA; EPQWAIG; -.
DR   OrthoDB; POG091H02GL; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP.
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; 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   PROSITE; PS00171; TIM_1; 1.
DR   PROSITE; PS51440; TIM_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3MIA6.
DR   SWISS-2DPAGE; C3MIA6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
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:ACP24454.1};
KW   Pentose shunt {ECO:0000256|HAMAP-Rule:MF_00147,
KW   ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728639};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   ACT_SITE     99     99       Electrophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00147}.
FT   ACT_SITE    172    172       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00147}.
FT   BINDING     178    178       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00147}.
FT   BINDING     215    215       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00147}.
SQ   SEQUENCE   261 AA;  28485 MW;  31744AF3D73D714A CRC64;
     MTGKSRFWIG TSWKMNKTLA EAEHFVRGLK AADATHDPRI QRFVIPAFTV LREVRAMLAQ
     TSVKVGAQNM HWADQGAWTG EVSPLMLKDC NLDLVELGHS ERREHFGETD ETVGLKTEAA
     VRHGLIPLIC VGETLRDRDS GNAPEVLAAQ VRGALSKLTA SQKTAEVLLA YEPVWAIGEK
     GIPATAEYAG ARQAEIIAVA EEVVGRKVPC LYGGSVNPQN CEELISSPHI DGLFIGRSAW
     NVEGYLDILA KCAAKLRGER E
//

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