6PGD_CHLTR
ID 6PGD_CHLTR Reviewed; 480 AA.
AC O84066;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE EC=1.1.1.44;
GN Name=gnd; OrderedLocusNames=CT_063;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate
CC to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP
CC to NADPH. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate
CC + NADPH; Xref=Rhea:RHEA:10116, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58121, ChEBI:CHEBI:58349, ChEBI:CHEBI:58759; EC=1.1.1.44;
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 3/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AE001273; AAC67654.1; -; Genomic_DNA.
DR PIR; A71561; A71561.
DR RefSeq; NP_219566.1; NC_000117.1.
DR RefSeq; WP_010725014.1; NC_000117.1.
DR AlphaFoldDB; O84066; -.
DR SMR; O84066; -.
DR STRING; 813.O172_00350; -.
DR EnsemblBacteria; AAC67654; AAC67654; CT_063.
DR GeneID; 884061; -.
DR KEGG; ctr:CT_063; -.
DR PATRIC; fig|272561.5.peg.72; -.
DR HOGENOM; CLU_024540_4_2_0; -.
DR InParanoid; O84066; -.
DR OMA; VIMVKAG; -.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR GO; GO:0046177; P:D-gluconate catabolic process; IBA:GO_Central.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006114; 6PGDH_C.
DR InterPro; IPR006113; 6PGDH_Gnd/GntZ.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR006184; 6PGdom_BS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006183; Pgluconate_DH.
DR PANTHER; PTHR11811; PTHR11811; 1.
DR Pfam; PF00393; 6PGD; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000109; 6PGD; 1.
DR PRINTS; PR00076; 6PGDHDRGNASE.
DR SMART; SM01350; 6PGD; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00873; gnd; 1.
DR PROSITE; PS00461; 6PGD; 1.
PE 3: Inferred from homology;
KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt;
KW Reference proteome.
FT CHAIN 1..480
FT /note="6-phosphogluconate dehydrogenase, decarboxylating"
FT /id="PRO_0000090033"
FT ACT_SITE 184
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 191
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 11..16
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 34..36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 76..78
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 130..132
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 187..188
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 454
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
SQ SEQUENCE 480 AA; 52667 MW; E2D9BFE893DCECB2 CRC64;
MAPNTDIGLI GLAVMGKNLV LNMVDHGFSV SVYNRSPAKT EEFLKDHGES GALQGFTTIQ
EFVQSLKRPR KIMIMIKAGA PVDEMIASLL PFLEEGDILI DGGNSYYLDS EQRYVDLKKE
GILFVGMGVS GGEEGARKGP SIMPGGNIDA WPAIAPIFQS IAAQVDGRPC CSWIGTGGAG
HFVKAVHNGI EYGDIQLICE TYEILKTRLN LSLEQIGNIF FEWNQTDLNS YLIGAAAAVL
IAKDENGNAI ASTILDVAGQ KGTGRWVAED AIKAGVPMSL IIESVLARYL STWKEVRTKA
AQEFPGIPLL CQPPQEASAF IEDVREALYA AKIISYAQGF MLLKQVSQDK GWDLNLGELA
LIWRGGCIIQ SAFLDKIHQG FENSPEAHSL ILQDYFKKVL FDSETGFRRA VLHAIGSGVA
IPCLSSALSF YDGYRTVDSS LFLVQGLRDY FGAHGYERRD CPRGEFYHTD WLETKKTFRV
