A9LZI9 (A9LZI9_NEIM0) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
6-phosphogluconate dehydrogenase, decarboxylating PIRNR PIRNR000109 RuleBase RU000485
EC=1.1.1.44 PIRNR PIRNR000109 RuleBase RU000485

Gene names

Name:	gnd EMBL ABX72247.1
Ordered Locus Names:	NMCC_0017

Organism

Neisseria meningitidis serogroup C (strain 053442) [Complete proteome] [HAMAP]

Taxonomic identifier

374833 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	470 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH By similarity. PIRNR PIRNR000109
Catalytic activity	6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH. PIRNR PIRNR000109 RuleBase RU000485
Pathway	Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3. PIRNR PIRNR000109 RuleBase RU004281
Subunit structure	Homodimer By similarity. PIRNR PIRNR000109
Sequence similarities	Belongs to the 6-phosphogluconate dehydrogenase family. PIRNR PIRNR000109 RuleBase RU000485

Ontologies

Keywords
Biological process	Gluconate utilization RuleBase RU000486 Pentose shunt PIRNR PIRNR000109 RuleBase RU004281
Ligand	NADP PIRNR PIRNR000109 RuleBase RU000485
Molecular function	Oxidoreductase PIRNR PIRNR000109 RuleBase RU000485
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	D-gluconate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW pentose-phosphate shunt Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro phosphogluconate dehydrogenase (decarboxylating) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Region	116 – 118	3	Substrate binding By similarity PIRSR PIRSR000109-2
	Region	174 – 175	2	Substrate binding By similarity PIRSR PIRSR000109-2
Sites
	Active site	171	1	Proton acceptor By similarity PIRSR PIRSR000109-1
	Active site	178	1	Proton donor By similarity PIRSR PIRSR000109-1
	Binding site	90	1	Substrate By similarity PIRSR PIRSR000109-2
	Binding site	179	1	Substrate By similarity PIRSR PIRSR000109-2
	Binding site	248	1	Substrate; via amide nitrogen By similarity PIRSR PIRSR000109-2
	Binding site	275	1	Substrate By similarity PIRSR PIRSR000109-2
	Binding site	433	1	Substrate; shared with dimeric partner By similarity PIRSR PIRSR000109-2
	Binding site	439	1	Substrate; shared with dimeric partner By similarity PIRSR PIRSR000109-2

Sequences

	Sequence		Length	Mass (Da)
	A9LZI9 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 1AE42A93737D4473	FASTA	470	51,765
	10 20 30 40 50 60 MGQNLILNMN DCGFKVVAYN RTIGKVDEFL NGAAKGTGII GAYSLQDLVD KLAKPRKIMM 70 80 90 100 110 120 MVRAGSVVDD FIEQLLPLLE EGDIIIDGGN ANYPDTTRRT HYLAEKGILF VGAGVSGGEE 130 140 150 160 170 180 GARHGPSIMP GGDKRAWEAV KPIFQAIAAK TPQGEPCCDW VGKDGAGHFV KMVHNGIEYG 190 200 210 220 230 240 DMQLICEAYQ FMKDGLGLSY DEMYRVFAEW NKTELDSYLI EITAAILGYK DEGGEPLVEK 250 260 270 280 290 300 ILDTAGQKGT GKWTGINALD LGIPLTLISE AVFARCVSSF KEQRVQTGKL FARTVTPVEG 310 320 330 340 350 360 GKQEWVEALR QALLASKIIS YAQGFMLIRE AGESYGWDLD YGNTALLWRE GCIIRSAFLS 370 380 390 400 410 420 NIRDAYENNP DLVFLGADPY FKNILENCLP AWRKVVAKAV ECGIPMPCMA SAITFLDGYT 430 440 450 460 470 TERLPANLLQ AQRDYFGAHT YERTDKPRGE FFHTNWTGKG GDTASTTYDI

References

[1]

"Characterization of ST-4821 complex, a unique Neisseria meningitidis clone." Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z., Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z., Liang X., Xu J., Jin Q. Genomics 91:78-87(2008) [PubMed: 18031983] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000381 Genomic DNA. Translation: ABX72247.1.
RefSeq	YP_001598200.1. NC_010120.1.
3D structure databases
ProteinModelPortal	A9LZI9.
SMR	A9LZI9. Positions 1-461.
ModBase	Search...
Protein-protein interaction databases
STRING	A9LZI9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBNEIT00000011987; EBNEIP00000011529; EBNEIG00000011987.
GeneID	5794950.
GenomeReviews	Gene locus NMCC_0017 in contig CP000381_GR.
KEGG	nmn:NMCC_0017.
PATRIC	20344156. VBINeiMen117761_0018.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000020474.
HOGENOM	HBG286913.
OMA	RAVENCQ.
ProtClustDB	PRK09287.
Enzyme and pathway databases
BioCyc	NMEN374833:NMCC_0017-MONOMER.
Family and domain databases
InterPro	IPR008927. 6-PGluconate_DH_C-like. IPR006114. 6PGDH_C. IPR006113. 6PGDH_decarbox. IPR006115. 6PGDH_NADP-bd. IPR006184. 6PGdom_BS. IPR013328. DH_multihelical. IPR012284. Fibritin/6PGD_C-extension. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:1.20.5.320. Fibritin/6PGD_C-extension. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
KO	K00033.
Pfam	PF00393. 6PGD. 1 hit. PF03446. NAD_binding_2. 1 hit. [Graphical view]
PIRSF	PIRSF000109. 6PGD. 1 hit.
SUPFAM	SSF48179. 6DGDH_C_like. 1 hit.
TIGRFAMs	TIGR00873. Gnd. 1 hit.
PROSITE	PS00461. 6PGD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

A9LZI9_NEIM0

Accession

Primary (citable) accession number: A9LZI9

Entry history

Integrated into UniProtKB/TrEMBL:	February 5, 2008
Last sequence update:	February 5, 2008
Last modified:	December 14, 2011
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)