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Database: UniProt
Entry: A0A0V1MRN0_9BILA
LinkDB: A0A0V1MRN0_9BILA
Original site: A0A0V1MRN0_9BILA 
ID   A0A0V1MRN0_9BILA        Unreviewed;       489 AA.
AC   A0A0V1MRN0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   28-MAR-2018, entry version 14.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
DE            EC=1.1.1.44 {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
GN   Name=T25B9.9 {ECO:0000313|EMBL:KRZ74386.1};
GN   ORFNames=T10_3623 {ECO:0000313|EMBL:KRZ74386.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ74386.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ74386.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ74386.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-
CC       phosphogluconate to ribulose 5-phosphate and CO(2), with
CC       concomitant reduction of NADP to NADPH.
CC       {ECO:0000256|PIRNR:PIRNR000109}.
CC   -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose
CC       5-phosphate + CO(2) + NADPH. {ECO:0000256|PIRNR:PIRNR000109,
CC       ECO:0000256|RuleBase:RU000485}.
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
CC       step 3/3. {ECO:0000256|PIRNR:PIRNR000109,
CC       ECO:0000256|RuleBase:RU000485}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000109}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase
CC       family. {ECO:0000256|PIRNR:PIRNR000109,
CC       ECO:0000256|RuleBase:RU000485}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KRZ74386.1}.
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DR   EMBL; JYDO01000051; KRZ74386.1; -; Genomic_DNA.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000054843; Unassembled WGS sequence.
DR   GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
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   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   Complete proteome {ECO:0000313|Proteomes:UP000054843};
KW   Gluconate utilization {ECO:0000256|RuleBase:RU000485};
KW   NADP {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000109,
KW   ECO:0000256|RuleBase:RU000485};
KW   Pentose shunt {ECO:0000256|PIRNR:PIRNR000109,
KW   ECO:0000256|RuleBase:RU000485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054843}.
FT   DOMAIN      183    476       6PGD. {ECO:0000259|SMART:SM01350}.
FT   NP_BIND      14     19       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   NP_BIND      37     39       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   NP_BIND      79     81       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   REGION      133    135       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   REGION      190    191       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   ACT_SITE    187    187       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   ACT_SITE    194    194       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   BINDING     107    107       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   BINDING     107    107       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     195    195       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     264    264       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     291    291       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     453    453       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     459    459       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
SQ   SEQUENCE   489 AA;  54120 MW;  CBB64A6969E15EE5 CRC64;
     MTMSAAEADI AVIGLAVMGQ NLILNMNDKG YVVCAFNRTV SKVDDFLNNE ARGTRVVGAH
     SLEEMAACLK RPRRVMLMVK AGSAVDDFID KLLTVLEKGD IIIDGGNSEY HDTQRRYTRL
     KEHGMHYVGC GVSGGEDGAR HGPSLMPGGA VEAWPHLKPI FQSIAAKVDD EPCCDWVGSD
     GAGHYVKMVH NGIEYGDMQL ISESYQFLRD VIGLNHDQMA DVFDRWNRTE LDSYLVELTA
     TVLRVKDKDG DPLVTKILDS AGQKGTGKWT AVSALDLGIP LSSIAEAVFA RCLSALVQDR
     KVASVRLPAS NQHLDPLNVE QQNDLIEHLR KALYVSKIVS YAQGFMMLQR ASAEYKWNLD
     YGKIALMWRG GCIIRSVFLN RIKQAFDRDT NIHNLLFDQF FSTAVKECQD SWRTIVSKSA
     LLGIPMPAFA STLAFYDGFR CVDLPASLLQ ALRDGFGAHT YQRKDNVGIF VHSDWTGHGG
     RTASSNYEV
//
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