(data stored in ACNUC7421 zone)

SWISSPROT: Q3Z539_SHISS

ID   Q3Z539_SHISS            Unreviewed;       335 AA.
AC   Q3Z539;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 83.
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:AAZ87123.1};
GN   OrderedLocusNames=SSON_0347 {ECO:0000313|EMBL:AAZ87123.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ87123.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ87123.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ87123.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ87123.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ87123; AAZ87123; SSON_0347.
DR   KEGG; ssn:SSON_0347; -.
DR   HOGENOM; HOG000020323; -.
DR   KO; K01698; -.
DR   OMA; GAWHDCG; -.
DR   Proteomes; UP000002529; 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; Q3Z539.
DR   SWISS-2DPAGE; Q3Z539.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002529};
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    206    206       Schiff-base intermediate with substrate.
FT                                {ECO:0000256|PIRSR:PIRSR001415-1}.
FT   ACT_SITE    258    258       Schiff-base intermediate with substrate.
FT                                {ECO:0000256|PIRSR:PIRSR001415-1}.
FT   METAL       131    131       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001415-3}.
FT   METAL       133    133       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001415-3}.
FT   METAL       141    141       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001415-3}.
FT   METAL       243    243       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR001415-5}.
FT   BINDING     216    216       Substrate 1. {ECO:0000256|PIRSR:
FT                                PIRSR001415-2}.
FT   BINDING     227    227       Substrate 1. {ECO:0000256|PIRSR:
FT                                PIRSR001415-2}.
FT   BINDING     284    284       Substrate 2. {ECO:0000256|PIRSR:
FT                                PIRSR001415-2}.
FT   BINDING     323    323       Substrate 2. {ECO:0000256|PIRSR:
FT                                PIRSR001415-2}.
SQ   SEQUENCE   335 AA;  36921 MW;  F8F93A16146B848D CRC64;
     MHLNSTNIRQ TMTDLIQRPR RLRKSPALRA MFEETTLSLN DLVLPIFVEE EIDDYKAVEA
     MPGVMRIPEK HLAREIERIA NAGIRSVMTF GISHHTDETG SDAWREDGLV ARMSRICKQT
     VPEMIVMSDT CFCEYTSHGH CGVLCEHGVD NDATLENLGK QAVVAAAAGA DFIAPSAAMD
     GQVQAIRQAL DAAGFKDTAI MSYSTKFASS FYGPFREAAG SALKGDRKSY QMNPMNRREA
     IRESLLDEAQ GADCLMVKPA GAYLDIVREL RERTELPIGA YQVSGEYAMI KFAALAGAID
     EEKVVLESLG SIKRAGADLI FSYFALDLAE KKILR
//

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