ID   HEM2_STAAR              Reviewed;         324 AA.
AC   Q6GG37;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 33.
DE   RecName: Full=Delta-aminolevulinic acid dehydratase;
DE            Short=ALADH;
DE            Short=ALAD;
DE            EC=4.2.1.24;
DE   AltName: Full=Porphobilinogen synthase;
GN   Name=hemB; OrderedLocusNames=SAR1748;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- CATALYTIC ACTIVITY: 2 5-aminolevulinate = porphobilinogen + 2
CC       H(2)O.
CC   -!- COFACTOR: Zinc (By similarity).
CC   -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis;
CC       coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC   -!- SUBUNIT: Homooctamer (By similarity).
CC   -!- SIMILARITY: Belongs to the ALADH family.
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DR   EMBL; BX571856; CAG40739.1; -; Genomic_DNA.
DR   RefSeq; YP_041135.1; -.
DR   GeneID; 2860701; -.
DR   GenomeReviews; BX571856_GR; SAR1748.
DR   KEGG; sar:SAR1748; -.
DR   HOGENOM; Q6GG37; -.
DR   OMA; Q6GG37; AESTPQF.
DR   BioCyc; SAUR282458:SAR1748-MON; -.
DR   GO; GO:0004655; F:porphobilinogen synthase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006779; P:porphyrin biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001731; 4pyrrol_synth_porphobiln_synth.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   PANTHER; PTHR11458; AlaD_dehydratase; 1.
DR   Pfam; PF00490; ALAD; 1.
DR   PIRSF; PIRSF001415; Porphbilin_synth; 1.
DR   PRINTS; PR00144; DALDHYDRTASE.
DR   ProDom; PD002304; AlaD_dehydratase; 1.
DR   PROSITE; PS00169; D_ALA_DEHYDRATASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Lyase; Porphyrin biosynthesis; Zinc.
FT   CHAIN         1    324       Delta-aminolevulinic acid dehydratase.
FT                                /FTId=PRO_0000140513.
FT   REGION      115    133       Zinc-binding (By similarity).
FT   ACT_SITE    248    248       By similarity.
SQ   SEQUENCE   324 AA;  36583 MW;  BF24378E01E7C93E CRC64;
     MKFDRHRRLR SSATMRDMVR ENHVRKEDLI YPIFVVEKDD VKKEIKSLPG VYQISLNLLE
     SELKEAYDLG IRAIMFFGVP NSKDDIGTGA YIHDGVIQQA TRIAKKMYDD LLIVADTCLC
     EYTDHGHCGV IDDHTHDVDN DKSLPLLVKT AISQVEAGAD IIAPSNMMDG FVAEIRRGLD
     EAGYYNIPIM SYGVKYASSF FGPFRDAADS APSFGDRKTY QMDPANRLEA LRELESDLKE
     GCDMMIVKPA LSYLDIVRDV KNHTNVPVVA YNVSGEYSMT KAAAQNGWID EERVVMEQMV
     SMKRAGADMI ITYFAKDICR YLDK
//