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Database: UniProt
Entry: E1VVX2_GLUAR
LinkDB: E1VVX2_GLUAR
Original site: E1VVX2_GLUAR 
ID   E1VVX2_GLUAR            Unreviewed;       479 AA.
AC   E1VVX2;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   28-MAR-2018, entry version 59.
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=gnd {ECO:0000313|EMBL:CBT75775.1};
GN   OrderedLocusNames=AARI_15520 {ECO:0000313|EMBL:CBT75775.1};
OS   Glutamicibacter arilaitensis (strain DSM 16368 / CIP 108037 / IAM
OS   15318 / JCM 13566 / Re117) (Arthrobacter arilaitensis).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae;
OC   Glutamicibacter.
OX   NCBI_TaxID=861360 {ECO:0000313|EMBL:CBT75775.1, ECO:0000313|Proteomes:UP000006878};
RN   [1] {ECO:0000313|EMBL:CBT75775.1, ECO:0000313|Proteomes:UP000006878}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC   {ECO:0000313|Proteomes:UP000006878};
RX   PubMed=21124797; DOI=10.1371/journal.pone.0015489;
RA   Monnet C., Loux V., Gibrat J.F., Spinnler E., Barbe V., Vacherie B.,
RA   Gavory F., Gourbeyre E., Siguier P., Chandler M., Elleuch R.,
RA   Irlinger F., Vallaeys T.;
RT   "The Arthrobacter arilaitensis Re117 genome sequence reveals its
RT   genetic adaptation to the surface of cheese.";
RL   PLoS ONE 5:E15489-E15489(2010).
RN   [2] {ECO:0000313|Proteomes:UP000006878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC   {ECO:0000313|Proteomes:UP000006878};
RA   Genoscope.;
RT   "Complete genome sequence of Arthrobacter arilaitensis (strain DSM
RT   16368 / CIP 108037 / JCM 13566 / Re117).";
RL   Submitted (JUL-2010) 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}.
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DR   EMBL; FQ311875; CBT75775.1; -; Genomic_DNA.
DR   RefSeq; WP_013348906.1; NC_014550.1.
DR   ProteinModelPortal; E1VVX2; -.
DR   STRING; 861360.AARI_15520; -.
DR   EnsemblBacteria; CBT75775; CBT75775; AARI_15520.
DR   KEGG; aai:AARI_15520; -.
DR   eggNOG; ENOG4105C7Q; Bacteria.
DR   eggNOG; COG0362; LUCA.
DR   HOGENOM; HOG000255147; -.
DR   KO; K00033; -.
DR   OMA; NSHYPDS; -.
DR   OrthoDB; POG091H01QF; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000006878; Chromosome.
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:UP000006878};
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, ECO:0000313|EMBL:CBT75775.1};
KW   Pentose shunt {ECO:0000256|PIRNR:PIRNR000109,
KW   ECO:0000256|RuleBase:RU000485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006878}.
FT   DOMAIN      179    467       6PGD. {ECO:0000259|SMART:SM01350}.
FT   NP_BIND       9     14       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   NP_BIND      32     34       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   NP_BIND      74     76       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   REGION      128    130       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   REGION      186    187       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   ACT_SITE    183    183       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   ACT_SITE    190    190       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   BINDING     102    102       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   BINDING     102    102       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     191    191       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     261    261       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     288    288       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     445    445       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     451    451       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
SQ   SEQUENCE   479 AA;  51278 MW;  57851EFB1CF93861 CRC64;
     MPAQIGVTGL AVMGANLARN FARNGYTVAL HNRSVGKTDA LLEAHGDEGD FIRTESLEEL
     VANLETPRRV LIMVKAGGPV DSVIDQLVPL LEEGDVVIDG GNSHYTDTRR REAALAEKGL
     HFVGIGVSGG EEGALLGPSI MPGGSAESYK SLGPMLEKIS AKADDGAPCC AWISTDGAGH
     FVKMVHNGIE YADMQVIGEA YDLMRSAAGI EPAKQAQIFN EWNQGELSSF LIEITAEVLG
     HTDAATGKPL VDVIQDSAGQ KGTGRWTVQS GLDMGSPVSA IAESVFARSL SSQRDIRAVG
     QEVLTGETAE VTLPENFVED VRQALFASKL VSYAQGIDML TSAAGEYNWE LKLDEIAGLW
     REGCIIRAAL LKDITAAYSA DEKPSNLLFA PAFAKAINDA VPAWRRVVSV AVQLGIPAPV
     FSSSLAYYDG LRRDRLPAAL TQGLRDYFGA HTYRRTDKEG TFHTLWSGDR TEIAAEDTH
//
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