A6SKR5 (A6SKR5_BOTFB) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Delta-aminolevulinic acid dehydratase RuleBase RU000515
EC=4.2.1.24 RuleBase RU000515

Gene names

ORF Names:

BC1G_13189 EMBL EDN19250.1

Organism

Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) [Complete proteome]

Taxonomic identifier

332648 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Leotiomycetes › Helotiales › Sclerotiniaceae › Botryotinia

Protein attributes

Sequence length	392 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	2 5-aminolevulinate = porphobilinogen + 2 H2O. RuleBase RU000515
Subunit structure	Homooctamer By similarity. PIRSR PIRSR001415-3 RuleBase RU000515
Sequence similarities	Belongs to the ALADH family. RuleBase RU004161

Ontologies

Keywords
Biological process	Porphyrin biosynthesis RuleBase RU000515
Ligand	Metal-binding PIRSR PIRSR001415-3 Zinc PIRSR PIRSR001415-3
Molecular function	Lyase RuleBase RU000515
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	porphyrin-containing compound biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW porphobilinogen synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Active site	262	1	Schiff-base intermediate with substrate By similarity PIRSR PIRSR001415-1
	Active site	315	1	Schiff-base intermediate with substrate By similarity PIRSR PIRSR001415-1
	Metal binding	185	1	Zinc; catalytic By similarity PIRSR PIRSR001415-3
	Metal binding	187	1	Zinc; catalytic By similarity PIRSR PIRSR001415-3
	Metal binding	195	1	Zinc; catalytic By similarity PIRSR PIRSR001415-3
	Binding site	272	1	Substrate 1 By similarity PIRSR PIRSR001415-2
	Binding site	284	1	Substrate 1 By similarity PIRSR PIRSR001415-2
	Binding site	342	1	Substrate 2 By similarity PIRSR PIRSR001415-2
	Binding site	381	1	Substrate 2 By similarity PIRSR PIRSR001415-2

Sequences

	Sequence		Length	Mass (Da)
	A6SKR5 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: FFAF601BE6EACB42	FASTA	392	42,501
	10 20 30 40 50 60 MSFSSLVQDL SFRDAASERR PPIRGPGSVS TYDDRASYVS RADSHVSRAR SYASTAATSV 70 80 90 100 110 120 SISGDIGSQL HGGYCHPLAR SWQAERQLTK SMLIYPLFIS DIEDEETLIP SLPDQHRRGI 130 140 150 160 170 180 NKVVPFLEPL VRKGLRSVIL FGVPIAPNVK DALGTAADDP QGPVIATIRL LRQRFPQLFI 190 200 210 220 230 240 VADVCLCEYT SHGHCGILRD DGSLNNQLSV DRVSDVAIAY AQAGAHCVAP SDMNDGRIRA 250 260 270 280 290 300 IKLKLIEEGI AHRVVLMSYA AKFSGCLYGP FRDAAGSVPS FGDRKCYQLP PGGRGLARRA 310 320 330 340 350 360 IERDIGEGAD IIMVKPASQY LDIISDAKEI GKNMPVAAYQ VSGEFAMIHA GAKAGVFDLK 370 380 390 TMAIESSEGI LRAGATIIVS YFTPQFLDWL ES

References

[1]

"Genomic analysis of the necrotrophic fungal pathogens Sclerotinia sclerotiorum and Botrytis cinerea." Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., Quevillon E. , Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M. PLoS Genet. 7:E1002230-E1002230(2011) [PubMed: 21876677] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: B05.10.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH476957 Genomic DNA. Translation: EDN19250.1.
RefSeq	XP_001548146.1. XM_001548096.1.
3D structure databases
ProteinModelPortal	A6SKR5.
SMR	A6SKR5. Positions 65-391.
ModBase	Search...
Protein-protein interaction databases
STRING	A6SKR5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5428627.
KEGG	bfu:BC1G_13189.
Phylogenomic databases
OMA	GAHCVAP.
OrthoDB	EOG454D75.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR001731. Porphobilinogen_synth. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K01698.
PANTHER	PTHR11458. AlaD_dehydratase. 1 hit.
Pfam	PF00490. ALAD. 1 hit. [Graphical view]
PIRSF	PIRSF001415. Porphbilin_synth. 1 hit.
PRINTS	PR00144. DALDHYDRTASE.
SMART	SM01004. ALAD. 1 hit. [Graphical view]
PROSITE	PS00169. D_ALA_DEHYDRATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

A6SKR5_BOTFB

Accession

Primary (citable) accession number: A6SKR5

Entry history

Integrated into UniProtKB/TrEMBL:	August 21, 2007
Last sequence update:	August 21, 2007
Last modified:	January 25, 2012
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)