RPIB_COCIM
ID RPIB_COCIM Reviewed; 163 AA.
AC P0CL19; A0A0E1RWN9; J3K544;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Putative ribose 5-phosphate isomerase;
DE EC=5.3.1.-;
GN ORFNames=CIMG_07932;
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 (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP SUBUNIT, AND ACTIVE SITE.
RX PubMed=21995815; DOI=10.1186/1472-6807-11-39;
RA Edwards T.E., Abramov A.B., Smith E.R., Baydo R.O., Leonard J.T.,
RA Leibly D.J., Thompkins K.B., Clifton M.C., Gardberg A.S., Staker B.L.,
RA Van Voorhis W.C., Myler P.J., Stewart L.J.;
RT "Structural characterization of a ribose-5-phosphate isomerase B from the
RT pathogenic fungus Coccidioides immitis.";
RL BMC Struct. Biol. 11:39-39(2011).
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000305|PubMed:21995815}.
CC -!- SIMILARITY: Belongs to the LacAB/RpiB family. {ECO:0000305}.
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DR EMBL; GG704913; EAS29186.1; -; Genomic_DNA.
DR RefSeq; XP_001240769.1; XM_001240768.1.
DR PDB; 3QD5; X-ray; 1.90 A; A/B=1-163.
DR PDB; 3SDW; X-ray; 1.80 A; A=1-163.
DR PDB; 3SGW; X-ray; 1.70 A; A=1-163.
DR PDBsum; 3QD5; -.
DR PDBsum; 3SDW; -.
DR PDBsum; 3SGW; -.
DR AlphaFoldDB; P0CL19; -.
DR SMR; P0CL19; -.
DR STRING; 246410.P0CL19; -.
DR EnsemblFungi; EAS29186; EAS29186; CIMG_07932.
DR GeneID; 4559626; -.
DR KEGG; cim:CIMG_07932; -.
DR VEuPathDB; FungiDB:CIMG_07932; -.
DR InParanoid; P0CL19; -.
DR OMA; DYPPFCL; -.
DR OrthoDB; 1421320at2759; -.
DR BRENDA; 5.3.1.6; 1544.
DR EvolutionaryTrace; P0CL19; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.1400.10; -; 1.
DR InterPro; IPR011860; Rib-5-P_Isoase_Actino.
DR InterPro; IPR003500; RpiB_LacA_LacB.
DR InterPro; IPR036569; RpiB_LacA_LacB_sf.
DR Pfam; PF02502; LacAB_rpiB; 1.
DR PIRSF; PIRSF005384; RpiB_LacA_B; 1.
DR SUPFAM; SSF89623; SSF89623; 1.
DR TIGRFAMs; TIGR02133; RPI_actino; 1.
DR TIGRFAMs; TIGR00689; rpiB_lacA_lacB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..163
FT /note="Putative ribose 5-phosphate isomerase"
FT /id="PRO_0000405565"
FT ACT_SITE 76
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:21995815,
FT ECO:0007744|PDB:3SGW"
FT BINDING 16..17
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000269|PubMed:21995815,
FT ECO:0007744|PDB:3SGW"
FT BINDING 77..81
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000269|PubMed:21995815,
FT ECO:0007744|PDB:3SGW"
FT BINDING 110
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT BINDING 120
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT BINDING 148
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:3SGW"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:3SGW"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:3SGW"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:3SGW"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:3SGW"
FT STRAND 70..79
FT /evidence="ECO:0007829|PDB:3SGW"
FT HELIX 80..87
FT /evidence="ECO:0007829|PDB:3SGW"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3SGW"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:3SGW"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:3SGW"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:3SGW"
FT HELIX 124..134
FT /evidence="ECO:0007829|PDB:3SGW"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:3SGW"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:3QD5"
SQ SEQUENCE 163 AA; 17399 MW; D1FC32D7DE695D1B CRC64;
MAATPLPPLR LAIACDDAGV SYKEALKAHL SDNPLVSSIT DVGVTSTTDK TAYPHVAIQA
AQLIKDGKVD RALMICGTGL GVAISANKVP GIRAVTAHDT FSVERAILSN DAQVLCFGQR
VIGIELAKRL AGEWLTYRFD QKSASAQKVQ AISDYEKKFV EVN
