A2R6C3 (A2R6C3_ASPNC) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Putative uncharacterized protein An15g07390 EMBL CAK48573.1
EC=1.1.1.8 EMBL CAK48573.1

Gene names

ORF Names:

An15g07390 EMBL CAK48573.1

Organism

Aspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]

Taxonomic identifier

425011 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Aspergillus niger

Protein attributes

Sequence length	414 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Sequence similarities

Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family. RuleBase RU000437

Ontologies

Keywords
Ligand	NAD RuleBase RU000437
Molecular function	Oxidoreductase RuleBase RU000437 EMBL CAK48573.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	NADH oxidation Inferred from electronic annotation. Source: EnsemblFungi glycerol metabolic process Inferred from electronic annotation. Source: EnsemblFungi glycerol-3-phosphate catabolic process Inferred from electronic annotation. Source: InterPro intracellular accumulation of glycerol Inferred from electronic annotation. Source: EnsemblFungi
Cellular_component	cytosol Inferred from electronic annotation. Source: EnsemblFungi glycerol-3-phosphate dehydrogenase complex Inferred from electronic annotation. Source: InterPro mitochondrion Inferred from electronic annotation. Source: EnsemblFungi nucleus Inferred from electronic annotation. Source: EnsemblFungi
Molecular_function	NAD binding Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate dehydrogenase [NAD+] activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	A2R6C3 [UniParc]. Last modified March 6, 2007. Version 1. Checksum: 5E64C900A03584EA	FASTA	414	45,449
	10 20 30 40 50 60 MHEHTRKHKV AVVGSGNWGS TISKIVAENA REHSDLFEPE VRMWVFEEEI EIPESSKHHS 70 80 90 100 110 120 KLGGQKHKLT EVINGVHENV KYLPDIALPE NVVADPDLKS AVKDATLLVF NLPHQFIGKT 130 140 150 160 170 180 LDGVVGHHLP YARGISCIKG VDVSDGTVTL HSELIMERLG IYCGALSGAN IAPEVAAEKF 190 200 210 220 230 240 CETTIGYDTP PMDVEERDGS PKENLIKIDE QRQHKTKPTH VKLHPVPKDL PPVDAELWET 250 260 270 280 290 300 LFARPYFHVN HVRDVAGVAL GGALKNIVAL ASGFVAGKGW GENAKAAIMR VGILEMIKFG 310 320 330 340 350 360 RTWFPKSVDE RTFTEESAGL ADVISSCSGG RNFRSACHAV EQGVSVNEIE QKELNGQKLQ 370 380 390 400 410 GTSTAYAVYD FLSKHDQLKE FPLFVAVHDI LEGKSTVDDL PALLDGKKKK NKSA

References

[1]

"Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88." Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M. , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H. Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CBS 513.88 / FGSC A1513.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM270351 Genomic DNA. Translation: CAK48573.1.
RefSeq	XP_001397265.1. XM_001397228.1.
3D structure databases
ProteinModelPortal	A2R6C3.
ModBase	Search...
Protein-protein interaction databases
STRING	5061.CADANGAP00012183.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANGAT00012418; CADANGAP00012183; CADANGAG00012418.
GeneID	4988340.
KEGG	ang:ANI_1_1768134.
Phylogenomic databases
HOGENOM	HOG000246855.
KO	K00006.
OrthoDB	EOG4FBN2Q.
Family and domain databases
Gene3D	1.10.1040.10. 1 hit. 3.40.50.720. 2 hits.
InterPro	IPR008927. 6-PGluconate_DH_C-like. IPR013328. DH_multihelical. IPR006168. G3P_DH_NAD-dep. IPR006109. G3P_DH_NAD-dep_C. IPR011128. G3P_DH_NAD-dep_N. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR11728. PTHR11728. 1 hit.
Pfam	PF07479. NAD_Gly3P_dh_C. 1 hit. PF01210. NAD_Gly3P_dh_N. 1 hit. [Graphical view]
PIRSF	PIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTS	PR00077. GPDHDRGNASE.
SUPFAM	SSF48179. 6DGDH_C_like. 1 hit.
PROSITE	PS00957. NAD_G3PDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

A2R6C3_ASPNC

Accession

Primary (citable) accession number: A2R6C3

Entry history

Integrated into UniProtKB/TrEMBL:	March 6, 2007
Last sequence update:	March 6, 2007
Last modified:	April 3, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)