(data stored in ACNUC7421 zone)

HOGENOM: NEIML_1_PE1

ID   NEIML_1_PE1                          STANDARD;      PRT;   482 AA.
AC   NEIML_1_PE1; C6S4B5;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; EC=1.1.1
DE   44; (NEIML_1.PE1).
GN   Name=gnd; OrderedLocusNames=NMO_0001;
OS   NEISSERIA MENINGITIDIS ALPHA14.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=662598;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS NEIML_1.PE1.
CC       Neisseria meningitidis alpha14, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C6S4B5_NEIML
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose
CC       5-phosphate + CO(2) + NADPH.
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
CC       step 3/3.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase
CC       family.
CC   -!- GENE_FAMILY: HOG000255147 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C6S4B5; -.
DR   EMBL; AM889136; CBA03303.1; -; Genomic_DNA.
DR   RefSeq; YP_003082250.1; NC_013016.1.
DR   ProteinModelPortal; C6S4B5; -.
DR   EnsemblBacteria; EBNEIT00000014560; EBNEIP00000014380; EBNEIG00000014560.
DR   GeneID; 8223026; -.
DR   GenomeReviews; AM889136_GR; NMO_0001.
DR   GeneTree; EBGT00050000020474; -.
DR   OMA; SNYPDTN; -.
DR   ProtClustDB; PRK09287; -.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:EC.
DR   GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-KW.
DR   InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR006114; 6PGDH_C.
DR   InterPro; IPR006113; 6PGDH_decarbox.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR006184; 6PGdom_BS.
DR   InterPro; IPR013328; DH_multihelical.
DR   InterPro; IPR012284; Fibritin/6PGD_C-extension.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:1.20.5.320; Fibritin/6PGD_C-extension; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1.
DR   Pfam; PF00393; 6PGD; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000109; 6PGD; 1.
DR   SUPFAM; SSF48179; 6DGDH_C_like; 1.
DR   TIGRFAMs; TIGR00873; Gnd; 1.
DR   PROSITE; PS00461; 6PGD; 1.
DR   HOGENOMDNA; NEIML_1.PE1; -.
KW   Complete proteome; Gluconate utilization; NADP; Oxidoreductase;
KW   Pentose shunt.
SQ   SEQUENCE   482 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKGDIGVIGL AVMGQNLILN MNDCGFKVVA YNRTIGKVDE FLNGAAKGTD IVGAYSLQDL
     VDKLAKPRKI MMMVRAGSVV DDFIEQLLPL LEEGDIVIDG GNANYPDTTR RTHYLAEKGI
     LFVGAGVSGG EEGARHGPSI MPGGDKRAWE AVKPIFQAIA AKTPQGEPCC DWVGKDGAGH
     FVKMVHNGIE YGDMQLICEA YQFMKDGLGL SYDEMHRVFA EWNKTELDSY LIEITAAILG
     YKDEGGEPLV EKILDTAGQK GTGKWTGINA LDLGIPLTLI SEAVFARCVS SFKEQRVQTG
     KLFARTVTPV EGGKQEWVEA LRQALLASKI ISYAQGFMLI REAGESYGWD LDYGNTALLW
     REGCIIRSAF LGNIRDAYEN NPDLVFLGED GYFKNILENC LPAWRRVVAK AVECGIPMPC
     MASAITFLDG YTTERLPANL LQAQRDYFGA HTYERTDKPR GEFFHTNWTG KGGDTASTTY
     DI
//

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