A5DVC4 (A5DVC4_LODEL) 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:

LELG_01310 EMBL EDK43132.1

Organism

Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) [Complete proteome]

Taxonomic identifier

379508 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Lodderomyces

Protein attributes

Sequence length	341 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)
	A5DVC4 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: 5BA30A10F3172062	FASTA	341	37,147
	10 20 30 40 50 60 MVHKAEFLPS TGNSISSILQ GGYNHPLSRE WQQERQLTKN MFIFPLFISD MPDDETDIPS 70 80 90 100 110 120 LPNIKRFGVN KLVPYVDSLV KKGLRAVILF GVPLKEGVKD SVGTAADDPE GPVITSIKLL 130 140 150 160 170 180 REKFPDLFIM CDVCLCEYTD HGHCGILNED GSLNREPSVR RIAAVAVNYA KAGAHSVAPS 190 200 210 220 230 240 DMMDGRIKDI KTGLMDAGLA HKCLVMSYAA KFSGNLYGPF RDAAGSAPSH GDRKAYQLPP 250 260 270 280 290 300 AGAGLARRAL LRDIEEGADA IMVKPSTFYL DIVSDASKLC GDYPLCAYHV SGEYAMLHAA 310 320 330 340 AEKGVVDLKG IAFEAHQGLV RAGARLIISY FTPEFLEWLD I

References

[1]

"Evolution of pathogenicity and sexual reproduction in eight Candida genomes." Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J. , Harris D., Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A. Nature 459:657-662(2009) [PubMed: 19465905] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 11503 / CBS 2605 / IFO 1676 / JCM 1781 / NRRL YB-4239 and ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH981524 Genomic DNA. Translation: EDK43132.1.
RefSeq	XP_001528790.1. XM_001528740.1.
3D structure databases
ProteinModelPortal	A5DVC4.
SMR	A5DVC4. Positions 2-340.
ModBase	Search...
Protein-protein interaction databases
STRING	A5DVC4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5234845.
KEGG	lel:LELG_01310.
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

A5DVC4_LODEL

Accession

Primary (citable) accession number: A5DVC4

Entry history

Integrated into UniProtKB/TrEMBL:	June 12, 2007
Last sequence update:	June 12, 2007
Last modified:	January 25, 2012
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)