(data stored in ACNUC7421 zone)

SWISSPROT: A0A0H3JFW2_ECO57

ID   A0A0H3JFW2_ECO57        Unreviewed;       335 AA.
AC   A0A0H3JFW2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   05-JUL-2017, entry version 11.
DE   RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515};
DE            EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515};
GN   OrderedLocusNames=ECs0423 {ECO:0000313|EMBL:BAB33846.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB33846.1, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB33846.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC   {ECO:0000313|Proteomes:UP000000558};
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- CATALYTIC ACTIVITY: 2 5-aminolevulinate = porphobilinogen + 2
CC       H(2)O. {ECO:0000256|RuleBase:RU000515}.
CC   -!- SUBUNIT: Homooctamer. {ECO:0000256|PIRSR:PIRSR001415-3,
CC       ECO:0000256|RuleBase:RU000515}.
CC   -!- SIMILARITY: Belongs to the ALAD family.
CC       {ECO:0000256|RuleBase:RU004161}.
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DR   EMBL; BA000007; BAB33846.1; -; Genomic_DNA.
DR   RefSeq; NP_308450.2; NC_002695.1.
DR   ProteinModelPortal; A0A0H3JFW2; -.
DR   STRING; 155864.Z0468; -.
DR   EnsemblBacteria; BAB33846; BAB33846; BAB33846.
DR   GeneID; 914525; -.
DR   KEGG; ecs:ECs0423; -.
DR   PATRIC; fig|386585.9.peg.518; -.
DR   KO; K01698; -.
DR   Proteomes; UP000000558; 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; A0A0H3JFW2.
DR   SWISS-2DPAGE; A0A0H3JFW2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000558};
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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