(data stored in SCRATCH zone)

SWISSPROT: C5BCB1_EDWI9

ID   C5BCB1_EDWI9            Unreviewed;       340 AA.
AC   C5BCB1;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 49.
DE   RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515};
DE            EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515};
GN   OrderedLocusNames=NT01EI_0147 {ECO:0000313|EMBL:ACR67402.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67402.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 2 5-aminolevulinate = porphobilinogen + 2
CC       H(2)O. {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; CP001600; ACR67402.1; -; Genomic_DNA.
DR   RefSeq; WP_015869618.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0147; -.
DR   EnsemblBacteria; ACR67402; ACR67402; NT01EI_0147.
DR   GeneID; 7958747; -.
DR   KEGG; eic:NT01EI_0147; -.
DR   PATRIC; fig|634503.3.peg.138; -.
DR   eggNOG; ENOG4105D52; Bacteria.
DR   eggNOG; COG0113; LUCA.
DR   HOGENOM; HOG000020323; -.
DR   KO; K01698; -.
DR   OMA; YQMDYAN; -.
DR   OrthoDB; POG091H03SU; -.
DR   Proteomes; UP000001485; 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; C5BCB1.
DR   SWISS-2DPAGE; C5BCB1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Lyase {ECO:0000256|RuleBase:RU000515, ECO:0000313|EMBL:ACR67402.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001415-5};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001415-5};
KW   Porphyrin biosynthesis {ECO:0000256|RuleBase:RU000515};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   ACT_SITE    204    204       Schiff-base intermediate with substrate.
FT                                {ECO:0000256|PIRSR:PIRSR001415-1}.
FT   ACT_SITE    259    259       Schiff-base intermediate with substrate.
FT                                {ECO:0000256|PIRSR:PIRSR001415-1}.
FT   METAL       244    244       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR001415-5}.
SQ   SEQUENCE   340 AA;  37512 MW;  F226F8C65E897D15 CRC64;
     MSYAFPGAFP GRRLRRLRRH DFSRRLCAEN VLTVDDLIYP VFVMEGNNHQ EAVSSMPGVQ
     RMTIDVLVRE AEAIAKLGVP VLSLFPVVGT DKKSLYAEEA YSSDGLVQRA VRALKDAVPE
     LGILTDVALD PYTTHGQDGV IDEDGYVVND ITKEILVRQA LSHAEAGADI VAPSDMMDGR
     IGAIRSMLED QKLVNTQIMA YSAKYASCYY GPFRDALGSS GNLKGGNKKT YQMDPANGDE
     ALQEVAQDLQ EGADMVMVKP GMPYLDVLRR VKDTFGVPTF AYQVSGEYAM HMAAIQNGWL
     QEKPAIMESL ICFKRAGADG VLTYFAKRVA QWLHDAEMNR
//

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