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Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
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

Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi129 – 1291Zinc; catalyticBy similarity
Metal bindingi131 – 1311Zinc; catalyticBy similarity
Metal bindingi139 – 1391Zinc; catalyticBy similarity
Active sitei204 – 2041Schiff-base intermediate with substrateBy similarity
Binding sitei214 – 2141Substrate 1By similarity
Binding sitei226 – 2261Substrate 1By similarity
Metal bindingi242 – 2421MagnesiumBy similarity
Active sitei257 – 2571Schiff-base intermediate with substrateBy similarity
Binding sitei283 – 2831Substrate 2By similarity
Binding sitei322 – 3221Substrate 2By similarity

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:MJ0643
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
ProteomesiUP000000805 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 335335Delta-aminolevulinic acid dehydratasePRO_0000140523Add
BLAST

Proteomic databases

PRIDEiQ60178.

Interactioni

Subunit structurei

Homooctamer.By similarity

Protein-protein interaction databases

STRINGi243232.MJ_0643.

Structurei

3D structure databases

ProteinModelPortaliQ60178.
SMRiQ60178. Positions 11-330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiCOG0113.
InParanoidiQ60178.
KOiK01698.
OMAiSTYQMDP.
PhylomeDBiQ60178.

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.

Q60178-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKINLGDFM LIRPRRLRKN QKIRDLVRET ILTKNDLIMP IFVDENLKGN
60 70 80 90 100
EKKEISSMPN QYRFSVEGAI EEAKEIADLG IPAVILFGIP KHKDEIASSA
110 120 130 140 150
YDKNGVVQRT IRGIKEELGD ELLVIADCCL CEYTSHGHCG IVKDGKILND
160 170 180 190 200
ATLPILAKIA LSYADAGVDI VAPSDMMDGR VRAIREILEE NGYDDVAIMS
210 220 230 240 250
YSAKYASSFY GPFREAAESA PKFGDRKSYQ MDIGNAREAL KEIALDIEEG
260 270 280 290 300
ADLILVKPAL PYLDIIRMAK DRFDVPIGGY CVSGEYAMVE AAARNGWLDR
310 320 330
EKVIYEILLS IKRAGADFII TYWAKEVAEI GLSQE
Length:335
Mass (Da):37,396
Last modified:November 1, 1997 - v1
Checksum:i4D097DAB45F3705D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98637.1.
PIRiC64380.
RefSeqiNP_247627.1. NC_000909.1.
WP_010870148.1. NC_000909.1.

Genome annotation databases

EnsemblBacteriaiAAB98637; AAB98637; MJ_0643.
GeneIDi1451509.
KEGGimja:MJ_0643.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98637.1.
PIRiC64380.
RefSeqiNP_247627.1. NC_000909.1.
WP_010870148.1. NC_000909.1.

3D structure databases

ProteinModelPortaliQ60178.
SMRiQ60178. Positions 11-330.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_0643.

Proteomic databases

PRIDEiQ60178.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB98637; AAB98637; MJ_0643.
GeneIDi1451509.
KEGGimja:MJ_0643.

Phylogenomic databases

eggNOGiCOG0113.
InParanoidiQ60178.
KOiK01698.
OMAiSTYQMDP.
PhylomeDBiQ60178.

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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.

Entry informationi

Entry nameiHEM2_METJA
AccessioniPrimary (citable) accession number: Q60178
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 24, 2015
This is version 97 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. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.