NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(92)90084-3; PubMed=1398086 [NCBI, ExPASy, EBI, Israel, Japan]
Broeckl G., Berchtold M., Behr M., Koenig H.;
"Sequence of the 5-aminolevulinic acid dehydratase-encoding gene from the hyperthermophilic methanogen, Methanothermus sociabilis.";
Gene 119:151-152(1992).

Comments

CATALYTIC ACTIVITY: 2 5-aminolevulinate = porphobilinogen + 2 H₂O.
COFACTOR: Zinc.
PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen III from 5-aminolevulinate: step 1/4 .
SUBUNIT: Homooctamer (By similarity).
SIMILARITY: Belongs to the ALADH family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M90083; AAA73226.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC1286; JC1286.

3D structure databases

HSSP

P13716; 1E51. [HSSP ENTRY / PDB]

ModBase

Q02250.

Ontologies

GO:0004655;	Molecular function: porphobilinogen synthase activity (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006779;	Biological process: porphyrin biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001731; 4pyrrol_synth_porphobiln_synth.
IPR013785; Aldolase_TIM.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

PANTHER

PTHR11458; AlaD_dehydratase; 1.

Pfam

PF00490; ALAD; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001415; Porphbilin_synth; 1.

PRINTS

PR00144; DALDHYDRTASE.

ProDom

PD002304; AlaD_dehydratase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00169; D_ALA_DEHYDRATASE; 1.

ProtoNet

Q02250.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Lyase; Porphyrin biosynthesis; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 320`	`320`	`Delta-aminolevulinic acid dehydratase.`	`PRO_0000140524`
`REGION`	`116 134`	`19`	`Zinc-binding (By similarity).`
`ACT_SITE`	`247 247`		`By similarity.`

Sequence information

Length: 320 AA [This is the length of the unprocessed precursor]

Molecular weight: 35925 Da [This is the MW of the unprocessed precursor]

CRC64: 16F13425105F38D0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKFPYTRMRR LRKNSKIRSL VKETTLSKDD LIYPVFVKEG IKTKEKIPKM PGQYRYSVDE 

        70         80         90        100        110        120 
LIDEAKKLEE KGLKAILVFG IPKKKDKYGS SAYDPNGIVQ KSVKLLKEET DLVVITDVCL 

       130        140        150        160        170        180 
CQYTEHGHCG IVKNKKIVND ETLKYLSKVA LSHAEAGADV VAPSDMMDGR VKAIREELEK 

       190        200        210        220        230        240 
NGFDDVIIMS YSAKYASSFY EPFRSAVYSS PAFGDRSTYQ MDPPNSLEAL REVKLDIDEG 

       250        260        270        280        290        300 
ADIVMVKPAL PYLDIIRLVK DTFGVPTAAY NVSGEYSMIK AAIDANYLSN KVIIETLLSI 

       310        320 
KRAGADLIIT HFAPEIVEEI

Q02250 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools