(data stored in ACNUC10821 zone)

SWISSPROT: C8U259_ECO10

ID   C8U259_ECO10            Unreviewed;       324 AA.
AC   C8U259;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 54.
DE   RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515};
DE            EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515};
GN   Name=hemB {ECO:0000313|EMBL:BAI29217.1};
GN   OrderedLocusNames=ECO103_0348 {ECO:0000313|EMBL:BAI29217.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29217.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29217.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen;
CC         Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24;
CC         Evidence={ECO:0000256|RuleBase:RU000515};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000256|RuleBase:RU000515}.
CC   -!- SIMILARITY: Belongs to the ALAD family.
CC       {ECO:0000256|RuleBase:RU004161}.
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DR   EMBL; AP010958; BAI29217.1; -; Genomic_DNA.
DR   RefSeq; WP_001295337.1; NC_013353.1.
DR   SMR; C8U259; -.
DR   EnsemblBacteria; BAI29217; BAI29217; ECO103_0348.
DR   KEGG; eoh:ECO103_0348; -.
DR   HOGENOM; HOG000020323; -.
DR   KO; K01698; -.
DR   OMA; GAWHDCG; -.
DR   BioCyc; ECOL585395:ECO103_RS01815-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004655; F:porphobilinogen synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR001731; ALAD.
DR   InterPro; IPR030656; ALAD_AS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   PANTHER; PTHR11458; PTHR11458; 1.
DR   Pfam; PF00490; ALAD; 1.
DR   PIRSF; PIRSF001415; Porphbilin_synth; 1.
DR   PRINTS; PR00144; DALDHYDRTASE.
DR   SMART; SM01004; ALAD; 1.
DR   PROSITE; PS00169; D_ALA_DEHYDRATASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U259.
DR   SWISS-2DPAGE; C8U259.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Lyase {ECO:0000256|RuleBase:RU000515};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001415-5};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001415-3};
KW   Porphyrin biosynthesis {ECO:0000256|RuleBase:RU000515};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001415-3}.
FT   ACT_SITE    195    195       Schiff-base intermediate with substrate.
FT                                {ECO:0000256|PIRSR:PIRSR001415-1}.
FT   ACT_SITE    247    247       Schiff-base intermediate with substrate.
FT                                {ECO:0000256|PIRSR:PIRSR001415-1}.
FT   METAL       120    120       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001415-3}.
FT   METAL       122    122       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001415-3}.
FT   METAL       130    130       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001415-3}.
FT   METAL       232    232       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR001415-5}.
FT   BINDING     205    205       Substrate 1. {ECO:0000256|PIRSR:
FT                                PIRSR001415-2}.
FT   BINDING     216    216       Substrate 1. {ECO:0000256|PIRSR:
FT                                PIRSR001415-2}.
FT   BINDING     273    273       Substrate 2. {ECO:0000256|PIRSR:
FT                                PIRSR001415-2}.
FT   BINDING     312    312       Substrate 2. {ECO:0000256|PIRSR:
FT                                PIRSR001415-2}.
SQ   SEQUENCE   324 AA;  35625 MW;  CE814E5705BFD255 CRC64;
     MTDLIQRPRR LRKSPALRAM FEETTLSLND LVLPIFVEEE IDDYKAVEAM PGVMRIPEKH
     LAREIERIAN AGIRSVMTFG ISHHTDETGS DAWREDGLVA RMSRICKQTV PEMIVMSDTC
     FCEYTSHGHC GVLCEHGVDN DATLENLGKQ AVVAAAAGAD FIAPSAAMDG QVQAIRQALD
     AAGFKDTAIM SYSTKFASSF YGPFREAAGS ALKGDRKSYQ MNPMNRREAI RESLLDEAQG
     ADCLMVKPAG AYLDIVRELR ERTELPIGAY QVSGEYAMIK FAALAGAIDE EKVVLESLGS
     IKRAGADLIF SYFALDLAEK KILR
//

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