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Q59643

- HEM2_PSEAE

UniProt

Q59643 - HEM2_PSEAE

Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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.1 Publication

    Enzyme regulationi

    Stimulated by magnesium ions.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei205 – 2051Schiff-base intermediate with substrate
    Binding sitei215 – 2151Substrate 1
    Binding sitei229 – 2291Substrate 1
    Metal bindingi245 – 2451Magnesium2 Publications
    Active sitei260 – 2601Schiff-base intermediate with substrate
    Binding sitei286 – 2861Substrate 2
    Binding sitei324 – 3241Substrate 2

    GO - Molecular functioni

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

    GO - Biological processi

    1. porphyrin-containing compound biosynthetic process Source: PseudoCAP
    2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Heme biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    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:PA5243
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002438: Chromosome

    Organism-specific databases

    PseudoCAPiPA5243.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 337337Delta-aminolevulinic acid dehydratasePRO_0000140507Add
    BLAST

    Interactioni

    Subunit structurei

    Homooctamer; formed by oligomerization of dimers.3 Publications

    Protein-protein interaction databases

    STRINGi208964.PA5243.

    Structurei

    Secondary structure

    1
    337
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni10 – 123
    Turni15 – 195
    Helixi22 – 287
    Helixi35 – 373
    Beta strandi38 – 4912
    Beta strandi51 – 533
    Beta strandi61 – 644
    Helixi65 – 7713
    Beta strandi82 – 876
    Helixi91 – 933
    Beta strandi95 – 973
    Helixi99 – 1024
    Helixi107 – 11812
    Beta strandi122 – 1287
    Turni131 – 1333
    Beta strandi134 – 1363
    Helixi150 – 16617
    Beta strandi170 – 1745
    Helixi181 – 19111
    Beta strandi198 – 2069
    Helixi209 – 2113
    Helixi212 – 2165
    Helixi221 – 2244
    Helixi229 – 2313
    Beta strandi232 – 2343
    Helixi240 – 25112
    Beta strandi255 – 2617
    Helixi263 – 2653
    Helixi266 – 27611
    Beta strandi280 – 2845
    Helixi286 – 29712
    Helixi305 – 31612
    Beta strandi319 – 3235
    Helixi326 – 3349

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B4KX-ray1.67A/B1-337[»]
    1GZGX-ray1.66A/B1-337[»]
    1W54X-ray2.20A/B1-337[»]
    1W56X-ray1.70A/B1-337[»]
    1W5MX-ray1.60A/B1-337[»]
    1W5NX-ray1.65A/B1-337[»]
    1W5OX-ray1.85A/B1-337[»]
    1W5PX-ray1.55A/B1-337[»]
    1W5QX-ray1.40A/B1-337[»]
    2C13X-ray2.15A/B1-337[»]
    2C14X-ray1.90A/B1-337[»]
    2C15X-ray1.48A/B1-337[»]
    2C16X-ray2.02A/B1-337[»]
    2C18X-ray1.93A/B1-337[»]
    2C19X-ray2.05A/B1-337[»]
    2WOQX-ray1.75A1-337[»]
    ProteinModelPortaliQ59643.
    SMRiQ59643. Positions 10-335.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ59643.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ALADH family.Curated

    Phylogenomic databases

    eggNOGiCOG0113.
    HOGENOMiHOG000020323.
    KOiK01698.
    OMAiMTILTHR.
    OrthoDBiEOG6VXFCB.
    PhylomeDBiQ59643.

    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]
    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.

    Q59643-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFTPANRAY PYTRLRRNRR DDFSRRLVRE NVLTVDDLIL PVFVLDGVNQ    50
    RESIPSMPGV ERLSIDQLLI EAEEWVALGI PALALFPVTP VEKKSLDAAE 100
    AYNPEGIAQR ATRALRERFP ELGIITDVAL DPFTTHGQDG ILDDDGYVLN 150
    DVSIDVLVRQ ALSHAEAGAQ VVAPSDMMDG RIGAIREALE SAGHTNVRIM 200
    AYSAKYASAY YGPFRDAVGS ASNLGKGNKA TYQMDPANSD EALHEVAADL 250
    AEGADMVMVK PGMPYLDIVR RVKDEFRAPT FVYQVSGEYA MHMGAIQNGW 300
    LAESVILESL TAFKRAGADG ILTYFAKQAA EQLRRGR 337
    Length:337
    Mass (Da):37,037
    Last modified:November 1, 1996 - v1
    Checksum:i7D650C49795D542C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91820 Genomic DNA. Translation: CAA62930.1.
    AE004091 Genomic DNA. Translation: AAG08628.1.
    PIRiS60577.
    RefSeqiNP_253930.1. NC_002516.2.

    Genome annotation databases

    EnsemblBacteriaiAAG08628; AAG08628; PA5243.
    GeneIDi879701.
    KEGGipae:PA5243.
    PATRICi19845337. VBIPseAer58763_5495.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91820 Genomic DNA. Translation: CAA62930.1 .
    AE004091 Genomic DNA. Translation: AAG08628.1 .
    PIRi S60577.
    RefSeqi NP_253930.1. NC_002516.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B4K X-ray 1.67 A/B 1-337 [» ]
    1GZG X-ray 1.66 A/B 1-337 [» ]
    1W54 X-ray 2.20 A/B 1-337 [» ]
    1W56 X-ray 1.70 A/B 1-337 [» ]
    1W5M X-ray 1.60 A/B 1-337 [» ]
    1W5N X-ray 1.65 A/B 1-337 [» ]
    1W5O X-ray 1.85 A/B 1-337 [» ]
    1W5P X-ray 1.55 A/B 1-337 [» ]
    1W5Q X-ray 1.40 A/B 1-337 [» ]
    2C13 X-ray 2.15 A/B 1-337 [» ]
    2C14 X-ray 1.90 A/B 1-337 [» ]
    2C15 X-ray 1.48 A/B 1-337 [» ]
    2C16 X-ray 2.02 A/B 1-337 [» ]
    2C18 X-ray 1.93 A/B 1-337 [» ]
    2C19 X-ray 2.05 A/B 1-337 [» ]
    2WOQ X-ray 1.75 A 1-337 [» ]
    ProteinModelPortali Q59643.
    SMRi Q59643. Positions 10-335.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 208964.PA5243.

    Protocols and materials databases

    DNASUi 879701.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG08628 ; AAG08628 ; PA5243 .
    GeneIDi 879701.
    KEGGi pae:PA5243.
    PATRICi 19845337. VBIPseAer58763_5495.

    Organism-specific databases

    PseudoCAPi PA5243.

    Phylogenomic databases

    eggNOGi COG0113.
    HOGENOMi HOG000020323.
    KOi K01698.
    OMAi MTILTHR.
    OrthoDBi EOG6VXFCB.
    PhylomeDBi Q59643.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00318 .

    Miscellaneous databases

    EvolutionaryTracei Q59643.

    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 ]
    PIRSFi PIRSF001415. Porphbilin_synth. 1 hit.
    PRINTSi PR00144. DALDHYDRTASE.
    SMARTi SM01004. ALAD. 1 hit.
    [Graphical view ]
    PROSITEi PS00169. D_ALA_DEHYDRATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, mapping and functional characterization of the hemB gene of Pseudomonas aeruginosa, which encodes a magnesium-dependent 5-aminolevulinic acid dehydratase."
      Frankenberg N., Kittel T., Hungerer C., Roemling U., Jahn D.
      Mol. Gen. Genet. 257:485-489(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
    3. "High resolution crystal structure of a Mg(2+)-dependent porphobilinogen synthase."
      Frankenberg N., Erskine P.T., Cooper J.B., Shoolingin-Jordan P.M., Jahn D., Heinz D.W.
      J. Mol. Biol. 289:591-602(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH LEVULINIC ACID AND MAGNESIUM, SUBUNIT.
    4. "Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism."
      Frere F., Schubert W.-D., Stauffer F., Frankenberg N., Neier R., Jahn D., Heinz D.W.
      J. Mol. Biol. 320:237-247(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF MUTANT ASN-139 IN COMPLEX WITH 5-FLUOROLEVULINIC ACID AND MAGNESIUM, COFACTOR, ACTIVE SITE.
    5. "Probing the active site of Pseudomonas aeruginosa porphobilinogen synthase using newly developed inhibitors."
      Frere F., Nentwich M., Gacond S., Heinz D.W., Neier R., Frankenberg-Dinkel N.
      Biochemistry 45:8243-8253(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM; 5-HYDROXYLEVULINIC ACID AND OTHER INHIBITORS, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE.
    6. "Structure of the heme biosynthetic Pseudomonas aeruginosa porphobilinogen synthase in complex with the antibiotic alaremycin."
      Heinemann I.U., Schulz C., Schubert W.D., Heinz D.W., Wang Y.G., Kobayashi Y., Awa Y., Wachi M., Jahn D., Jahn M.
      Antimicrob. Agents Chemother. 54:267-272(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH ALAREMYCIN.

    Entry informationi

    Entry nameiHEM2_PSEAE
    AccessioniPrimary (citable) accession number: Q59643
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 110 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3