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Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity).By similarity

Catalytic activityi

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per monomer.By similarity

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Delta-aminolevulinic acid dehydratase (hemB)
  2. Probable porphobilinogen deaminase (hemC)
  3. Putative uroporphyrinogen-III synthase (hemD)
  4. no protein annotated in this organism
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate, the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi125Zinc; catalyticBy similarity1
Metal bindingi127Zinc; catalyticBy similarity1
Metal bindingi135Zinc; catalyticBy similarity1
Active sitei200Schiff-base intermediate with substrateBy similarity1
Binding sitei210Substrate 1By similarity1
Binding sitei222Substrate 1By similarity1
Metal bindingi238MagnesiumBy similarity1
Active sitei253Schiff-base intermediate with substrateBy similarity1
Binding sitei279Substrate 2By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-aminolevulinic acid dehydratase (EC:4.2.1.24)
Short name:
ALAD
Short name:
ALADH
Alternative name(s):
Porphobilinogen synthase
Gene namesi
Name:hemB
Ordered Locus Names:MTH_744
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000005223 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001405251 – 326Delta-aminolevulinic acid dehydrataseAdd BLAST326

Interactioni

Subunit structurei

Homooctamer.By similarity

Protein-protein interaction databases

STRINGi187420.MTH744.

Structurei

3D structure databases

ProteinModelPortaliO26839.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiarCOG04300. Archaea.
COG0113. LUCA.
KOiK01698.
OMAiMDPANSN.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR001731. ALAD.
IPR030656. ALAD_AS.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERiPTHR11458. PTHR11458. 1 hit.
PfamiPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSiPR00144. DALDHYDRTASE.
SMARTiSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O26839-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDNMEFPTK RMRRLRKSPQ IRNILRETRL HPSDLIYPMF VSEKLGRGDV
60 70 80 90 100
EAIDTMPGQF RYSVDDAVSE ASRLEDEGLS SVLIFGMPSA KDELASAAHD
110 120 130 140 150
PHGVVQRTVR RLKEETDLVV MTDVCLCQYT SHGHCGIVVD GEIVNDETLE
160 170 180 190 200
VLSRIALSHA EAGADVVAPS DMMDGRVAAI RRSLDDAGFQ DTLIMSYAVK
210 220 230 240 250
YASAFYAPFR GAVSSAPAFG DRRSYQMDPA NIDEALIEAE LDLREGADIL
260 270 280 290 300
MVKPALAYLD VIGKVRERFS VPLAAYNVSG EYSMLKAAIK SGYLTDEAIY
310 320
ESILSIKRAG ADLIISHFAP DLLGVI
Length:326
Mass (Da):35,841
Last modified:January 1, 1998 - v1
Checksum:i29EDC9060F39A170
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB85248.1.
PIRiE69199.

Genome annotation databases

EnsemblBacteriaiAAB85248; AAB85248; MTH_744.
KEGGimth:MTH_744.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB85248.1.
PIRiE69199.

3D structure databases

ProteinModelPortaliO26839.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi187420.MTH744.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB85248; AAB85248; MTH_744.
KEGGimth:MTH_744.

Phylogenomic databases

eggNOGiarCOG04300. Archaea.
COG0113. LUCA.
KOiK01698.
OMAiMDPANSN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR001731. ALAD.
IPR030656. ALAD_AS.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERiPTHR11458. PTHR11458. 1 hit.
PfamiPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSiPR00144. DALDHYDRTASE.
SMARTiSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHEM2_METTH
AccessioniPrimary (citable) accession number: O26839
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.