A2C1K6 (A2C1K6_PROM1) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

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

Gene names

Name:	gnd EMBL ABM75366.1
Ordered Locus Names:	NATL1_08081

Organism

Prochlorococcus marinus (strain NATL1A) [Complete proteome] [HAMAP] EMBL ABM75366.1

Taxonomic identifier

167555 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length	472 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
Pathway	Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3. PIRNR PIRNR000109
Subunit structure	Homodimer By similarity. PIRNR PIRNR000109
Sequence similarities	Belongs to the 6-phosphogluconate dehydrogenase family. PIRNR PIRNR000109

Ontologies

Keywords
Biological process	Pentose shunt PIRNR PIRNR000109
Ligand	NADP PIRNR PIRNR000109
Molecular function	Oxidoreductase PIRNR PIRNR000109 EMBL ABM75366.1
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
	Nucleotide binding	10 – 15	6	NADP By similarity PIRSR PIRSR000109-3
	Nucleotide binding	33 – 35	3	NADP By similarity PIRSR PIRSR000109-3
	Nucleotide binding	75 – 77	3	NADP By similarity PIRSR PIRSR000109-3
	Region	129 – 131	3	Substrate binding By similarity PIRSR PIRSR000109-2
	Region	186 – 187	2	Substrate binding By similarity PIRSR PIRSR000109-2
Sites
	Active site	183	1	Proton acceptor By similarity PIRSR PIRSR000109-1
	Active site	190	1	Proton donor By similarity PIRSR PIRSR000109-1
	Binding site	103	1	NADP By similarity PIRSR PIRSR000109-3
	Binding site	103	1	Substrate By similarity PIRSR PIRSR000109-2
	Binding site	191	1	Substrate By similarity PIRSR PIRSR000109-2
	Binding site	262	1	Substrate; via amide nitrogen By similarity PIRSR PIRSR000109-2
	Binding site	289	1	Substrate By similarity PIRSR PIRSR000109-2
	Binding site	449	1	Substrate; shared with dimeric partner By similarity PIRSR PIRSR000109-2
	Binding site	455	1	Substrate; shared with dimeric partner By similarity PIRSR PIRSR000109-2

Sequences

	Sequence		Length	Mass (Da)
	A2C1K6 [UniParc]. Last modified February 20, 2007. Version 1. Checksum: E60C9C407621688F	FASTA	472	51,466
	10 20 30 40 50 60 MTKAHFGLVG LGVMGENLVL NAERNGFSSV VYNRTYQKTE DFLLGRGVNK SIQGAKDLQE 70 80 90 100 110 120 FVSKLERPRR VLMMVKAGAA TDAVINQISP FLEEGDLLID GGNAQFMDTE RRVKELESKS 130 140 150 160 170 180 FGYIGMGVSG GAKGALEGPS MMPGGTKTSY DAIESLLNKM AAQVEDGPCV TYIGPGGSGH 190 200 210 220 230 240 FVKTVHNGIE YGIEQILAEA YDLMKRVCGM SGDEMASVMG YWNKTEELSS YLVEITEACL 250 260 270 280 290 300 RVKDPDDSSD LVEKIMDKAG QKGTGLWTVV SALELGASVP TIYASLNGRV MSSMKDQRNY 310 320 330 340 350 360 AETILNGNKP SFVDFGKPSD GMPLLMDAVV LATIASYAQG MDILRLASEE YDYDLDMPSI 370 380 390 400 410 420 AQIWKGGCII RSTLLSRIQD AFKKDPSLTN LIIDKWFTDQ VNNRLSGLTQ VVSAAANAGI 430 440 450 460 470 PVPCLSSTLD YLNSFRTSRL PQNLVQAMRD CFGSHTYERV DKAGSFHTEW ID

References

[1]

"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus." Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W. PLoS Genet. 3:2515-2528(2007) [PubMed: 18159947] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000553 Genomic DNA. Translation: ABM75366.1.
RefSeq	YP_001014631.1. NC_008819.1.
3D structure databases
ProteinModelPortal	A2C1K6.
ModBase	Search...
Protein-protein interaction databases
STRING	A2C1K6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4781048.
GenomeReviews	Gene locus NATL1_08081 in contig CP000553_GR.
KEGG	pme:NATL1_08081.
PATRIC	23019191. VBIProMar31285_0825.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0362.
HOGENOM	HBG286913.
OMA	MEHNEMA.
PhylomeDB	A2C1K6.
ProtClustDB	PRK09287.
Enzyme and pathway databases
BioCyc	PMAR167555:NATL1_08081-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

A2C1K6_PROM1

Accession

Primary (citable) accession number: A2C1K6

Entry history

Integrated into UniProtKB/TrEMBL:	February 20, 2007
Last sequence update:	February 20, 2007
Last modified:	January 25, 2012
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)