Q6C0Y3 (Q6C0Y3_YARLI) 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

Ordered Locus Names:

YALI0F20790g

Organism

Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)

Taxonomic identifier

284591 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia

Protein attributes

Sequence length	342 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 Reference 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	210	1	Schiff-base intermediate with substrate By similarity PIRSR PIRSR001415-1
	Active site	263	1	Schiff-base intermediate with substrate By similarity PIRSR PIRSR001415-1
	Metal binding	134	1	Zinc; catalytic By similarity PIRSR PIRSR001415-3
	Metal binding	136	1	Zinc; catalytic By similarity PIRSR PIRSR001415-3
	Metal binding	144	1	Zinc; catalytic By similarity PIRSR PIRSR001415-3
	Binding site	220	1	Substrate 1 By similarity PIRSR PIRSR001415-2
	Binding site	232	1	Substrate 1 By similarity PIRSR PIRSR001415-2
	Binding site	290	1	Substrate 2 By similarity PIRSR PIRSR001415-2
	Binding site	329	1	Substrate 2 By similarity PIRSR PIRSR001415-2

Sequences

	Sequence		Length	Mass (Da)
	Q6C0Y3 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 5CDA913318FBD212	FASTA	342	37,525
	10 20 30 40 50 60 MVHKAEYLEE HETQISSILS GGYAHPLSRQ WQQKNRLTKD MFIYPLFVTD DPEEETPISS 70 80 90 100 110 120 LPGQKRWGVN KLVPYVDSLV KKGLRSVILF GVPMKEGVKD LEGTAADDPE GPVIQATKAL 130 140 150 160 170 180 KKAFPDLFVM CDVCLCEYTS HGHCGVLRED GTVIRDTTVR RLAAVAVNYA KAGADCVAPS 190 200 210 220 230 240 DMIDGRIHDI KKGLLKAGLA HNVMVMSYTK FSGNLYGPFR EAACSAPSHG DRKRYQLPAG 250 260 270 280 290 300 GRGLARRALA RDLAEGADAV IVKPSTFYLD IVVDAAEICK DVPIATYQVS GEYAMIHAAA 310 320 330 340 EKGVVDLEVM AFEAAYGNLR AGANLLISYF TPDFLEWLDH HH

References

[1]

"Genome evolution in yeasts." Genolevures Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIB 122 / E 150.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382132 Genomic DNA. Translation: CAG78488.1.
RefSeq	XP_505679.1. XM_505679.1.
3D structure databases
ProteinModelPortal	Q6C0Y3.
SMR	Q6C0Y3. Positions 2-339.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6C0Y3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2908950.
GenomeReviews	Gene locus YALI0F20790g in contig CR382132_GR.
KEGG	yli:YALI0F20790g.
Phylogenomic databases
eggNOG	fuNOG07497.
HOGENOM	HBG285270.
OMA	XDERGSA.
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

Q6C0Y3_YARLI

Accession

Primary (citable) accession number: Q6C0Y3

Entry history

Integrated into UniProtKB/TrEMBL:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)