TPIS_COCIM
ID TPIS_COCIM Reviewed; 289 AA.
AC P0CL22; J3K4F8; J3K545;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Putative triosephosphate isomerase;
DE Short=TIM;
DE EC=5.3.1.1;
DE AltName: Full=Triose-phosphate isomerase;
GN ORFNames=CIMG_07933;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of a putative triosephosphate isomerase from
RT Coccidioides immitis.";
RL Submitted (JUN-2010) to the PDB data bank.
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:0000255|PROSITE-ProRule:PRU10127};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate from glycerone phosphate: step 1/1. {ECO:0000255|PROSITE-
CC ProRule:PRU10127}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000255|PROSITE-ProRule:PRU10127}.
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DR EMBL; GG704913; EAS29187.3; -; Genomic_DNA.
DR RefSeq; XP_001240770.1; XM_001240769.2.
DR PDB; 3S6D; X-ray; 2.20 A; A=1-289.
DR PDBsum; 3S6D; -.
DR AlphaFoldDB; P0CL22; -.
DR SMR; P0CL22; -.
DR STRING; 246410.P0CL22; -.
DR EnsemblFungi; EAS29187; EAS29187; CIMG_07933.
DR GeneID; 4559627; -.
DR KEGG; cim:CIMG_07933; -.
DR VEuPathDB; FungiDB:CIMG_07933; -.
DR InParanoid; P0CL22; -.
DR OMA; CIGEKTH; -.
DR OrthoDB; 1272577at2759; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; P0CL22; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 CDD; cd00311; TIM; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035990; TIM_sf.
DR InterPro; IPR000652; Triosephosphate_isomerase.
DR PANTHER; PTHR21139; PTHR21139; 1.
DR Pfam; PF00121; TIM; 1.
DR SUPFAM; SSF51351; SSF51351; 1.
DR PROSITE; PS51440; TIM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase;
KW Reference proteome.
FT CHAIN 1..289
FT /note="Putative triosephosphate isomerase"
FT /id="PRO_0000405777"
FT ACT_SITE 127
FT /note="Electrophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:3S6D"
FT HELIX 28..39
FT /evidence="ECO:0007829|PDB:3S6D"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:3S6D"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3S6D"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:3S6D"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:3S6D"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3S6D"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:3S6D"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:3S6D"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:3S6D"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:3S6D"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:3S6D"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:3S6D"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:3S6D"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:3S6D"
FT HELIX 169..190
FT /evidence="ECO:0007829|PDB:3S6D"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:3S6D"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:3S6D"
FT HELIX 215..233
FT /evidence="ECO:0007829|PDB:3S6D"
FT STRAND 240..248
FT /evidence="ECO:0007829|PDB:3S6D"
FT TURN 250..256
FT /evidence="ECO:0007829|PDB:3S6D"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:3S6D"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:3S6D"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:3S6D"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:3S6D"
SQ SEQUENCE 289 AA; 31418 MW; B9E2A468EC1E5DB0 CRC64;
MASALAGPRF PPLPKTLLII SLKMYFTPSR TIDYIQGLLE PRNDIIRQEN RSRLLLALIP
DFLTIYPCSE AIKEFESNLA APQDADTPPP LLLGAQDCFW DSLGPYTGEI SPVCLRDMNV
SIVELGHAER RAIFGETDQQ VARKAAAAAD QGLIPLVCIG EVSTLGPIVS EAIGRAVGEC
EAQIRPVLEA LPRDAPVIFA YEPVWAIGKP QPARVDHVGA VVSGIRSVIE RIDRHRKGEV
RILYGGSAGP GLWGPGGLGK EVDGMFLGRF AHDIEGVRKV VREVEESLR
