Q6CKN7 (Q6CKN7_KLULA) 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:

KLLA0F09273g

Organism

Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

284590 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

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
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	211	1	Schiff-base intermediate with substrate By similarity PIRSR PIRSR001415-1
	Active site	264	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	221	1	Substrate 1 By similarity PIRSR PIRSR001415-2
	Binding site	233	1	Substrate 1 By similarity PIRSR PIRSR001415-2
	Binding site	291	1	Substrate 2 By similarity PIRSR PIRSR001415-2
	Binding site	330	1	Substrate 2 By similarity PIRSR PIRSR001415-2

Sequences

	Sequence		Length	Mass (Da)
	Q6CKN7 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: EE156A69483C81D6	FASTA	342	37,947
	10 20 30 40 50 60 MVHVARFLDE RPTDIPSILA GGYNHPLLRE WQNERQLTKN MFIFPLFVSD QDDEETIIPS 70 80 90 100 110 120 LPNIKRFGIN RLKDYVAGLV AKGLRSVILF GVPLKDGAKD QVATSADDPE GPVIQAIKLL 130 140 150 160 170 180 RKEFPDLYII CDVCLCEYTS HGHCGVLYED GTINREKSVQ RIAAVAVNYA IAGAHCVAPS 190 200 210 220 230 240 DMIDGRIREI KMGLIEHGLA HKTFVMSYSA KFSGNLYGPF RDAACSQPGK GDRKCYQLPS 250 260 270 280 290 300 GGRGLARRAL KRDLQEGSDG IIVKPSTFYL DVMSDAAEIC RDLPVCAYHV SGEYAMLHAA 310 320 330 340 AEKGVVDLKS IAFESHYGFL RAGARLIISY FTPEFLEWLD EN

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: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382126 Genomic DNA. Translation: CAG98210.1.
RefSeq	XP_455502.1. XM_455502.1.
3D structure databases
ProteinModelPortal	Q6CKN7.
SMR	Q6CKN7. Positions 2-341.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6CKN7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2896036.
GenomeReviews	Gene locus KLLA0F09273g in contig CR382126_GR.
KEGG	kla:KLLA0F09273g.
Phylogenomic databases
eggNOG	fuNOG07497.
HOGENOM	HBG285270.
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

Q6CKN7_KLULA

Accession

Primary (citable) accession number: Q6CKN7

Entry history

Integrated into UniProtKB/TrEMBL:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)