(data stored in SCRATCH zone)

SWISSPROT: D3UZ79_XENBS

ID   D3UZ79_XENBS            Unreviewed;       338 AA.
AC   D3UZ79;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, 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   Name=hemB {ECO:0000313|EMBL:CBJ79661.1};
GN   OrderedLocusNames=XBJ1_0512 {ECO:0000313|EMBL:CBJ79661.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79661.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79661.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79661.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; FN667741; CBJ79661.1; -; Genomic_DNA.
DR   RefSeq; WP_012987117.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0512; -.
DR   EnsemblBacteria; CBJ79661; CBJ79661; XBJ1_0512.
DR   GeneID; 8830135; -.
DR   KEGG; xbo:XBJ1_0512; -.
DR   PATRIC; fig|406818.4.peg.472; -.
DR   eggNOG; ENOG4105D52; Bacteria.
DR   eggNOG; COG0113; LUCA.
DR   HOGENOM; HOG000020323; -.
DR   KO; K01698; -.
DR   OMA; YQMDYAN; -.
DR   BioCyc; XBOV406818:XBJ1_RS02215-MONOMER; -.
DR   Proteomes; UP000002045; 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; D3UZ79.
DR   SWISS-2DPAGE; D3UZ79.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Lyase {ECO:0000256|RuleBase:RU000515, ECO:0000313|EMBL:CBJ79661.1};
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:UP000002045}.
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   338 AA;  37675 MW;  D5373DBBB51218A5 CRC64;
     MSYVFPGTFP GRRMRRVRRH DFSRRLVAEN QLTVNDLIYP VFVMEGINQR QEVSSMPGVY
     RLTIDLLLKE AEEIARLGIP VLSLFPAIEA DKKSLDAQES YNPDGLIQRS IRALKNEVPE
     LGLLTDVALD PFTTHGQDGV IDQDGYVIND ITKEILVKQA LSHAEAGAEI VAPSDMMDGR
     IGAIRDQLEV DGYINTQIMA YSAKYASCYY GPFRDAIGSS GNLKGGNKMT YQMDPANSDE
     ALQEIAQDLQ EGADSVMVKP GMPYLDVIRR VKDTFGVPTF AYQVSGEYAM HVAAIQNGWL
     KEQPAIMESL LCFKRAGADG VLTYFAKRVA QWLNEQKY
//

If you have problems or comments...

PBIL Back to PBIL home page