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Q59295

- HEM2_CLOJO

UniProt

Q59295 - HEM2_CLOJO

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Protein
Delta-aminolevulinic acid dehydratase
Gene
hemB
Organism
Clostridium josui
Status
Reviewed - 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.

Catalytic activityi

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactori

Binds 1 zinc ion per monomer By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi117 – 1171Zinc; catalytic By similarity
Metal bindingi119 – 1191Zinc; catalytic By similarity
Metal bindingi127 – 1271Zinc; catalytic By similarity
Active sitei192 – 1921Schiff-base intermediate with substrate By similarity
Binding sitei202 – 2021Substrate By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. porphobilinogen synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

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
OrganismiClostridium josui
Taxonomic identifieri1499 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›205›205Delta-aminolevulinic acid dehydratase
PRO_0000140500Add
BLAST

Proteomic databases

PRIDEiQ59295.

Interactioni

Subunit structurei

Homooctamer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ59295.

Family & Domainsi

Sequence similaritiesi

Belongs to the ALADH family.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view]
PANTHERiPTHR11458. PTHR11458. 1 hit.
PfamiPF00490. ALAD. 1 hit.
[Graphical view]
PRINTSiPR00144. DALDHYDRTASE.
SMARTiSM01004. ALAD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q59295-1 [UniParc]FASTAAdd to Basket

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MIKRPRRLRT NEVLRKAVRE TRLSTDSLIW PLFIVEGKNI KKEISSLPGQ    50
YHFSPDMVGK AIEAALKADV KSVLLFGLPK HKDEKGSEAY NENGVLQQGI 100
REIKQRYPQM QVITDICMCE YTSHGHCGIL EGERVDNDRT LPYLEKIALS 150
HVMAGADMIA PSDMMDGRIY ALRSTLDKNG FTDIPIMSYA VKYASSFYGP 200
FREAA 205
Length:205
Mass (Da):23,172
Last modified:November 1, 1997 - v1
Checksum:i886F9DAEFDB1144E
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei205 – 2051

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D28503 Genomic DNA. Translation: BAA05863.1.
PIRiI40812.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D28503 Genomic DNA. Translation: BAA05863.1 .
PIRi I40812.

3D structure databases

ProteinModelPortali Q59295.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q59295.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00318 .

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view ]
PANTHERi PTHR11458. PTHR11458. 1 hit.
Pfami PF00490. ALAD. 1 hit.
[Graphical view ]
PRINTSi PR00144. DALDHYDRTASE.
SMARTi SM01004. ALAD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and sequencing of some genes responsible for porphyrin biosynthesis from the anaerobic bacterium Clostridium josui."
    Fujino E., Fujino T., Karita S., Sakka K., Ohmiya K.
    J. Bacteriol. 177:5169-5175(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: FERM P-9684.

Entry informationi

Entry nameiHEM2_CLOJO
AccessioniPrimary (citable) accession number: Q59295
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

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

External Data

Dasty 3

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