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   27-MAR-2024, entry version 101.
DE   RecName: Full=Delta-aminolevulinic acid dehydratase;
DE            Short=ALAD;
DE            Short=ALADH;
DE            EC=4.2.1.24;
DE   AltName: Full=Porphobilinogen synthase;
GN   Name=hemB; OrderedLocusNames=SAR1748;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
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., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles.
CC       Binds two molecules of 5-aminolevulinate per subunit, each at a
CC       distinct site, and catalyzes their condensation to form porphobilinogen
CC       (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000250};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC   -!- SUBUNIT: Homooctamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000305}.
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; BX571856; CAG40739.1; -; Genomic_DNA.
DR   RefSeq; WP_000667126.1; NC_002952.2.
DR   AlphaFoldDB; Q6GG37; -.
DR   SMR; Q6GG37; -.
DR   KEGG; sar:SAR1748; -.
DR   HOGENOM; CLU_035731_0_0_9; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000000596; 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:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00384; ALAD_PBGS; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR001731; ALAD.
DR   InterPro; IPR030656; ALAD_AS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   PANTHER; PTHR11458; DELTA-AMINOLEVULINIC ACID DEHYDRATASE; 1.
DR   PANTHER; PTHR11458:SF0; DELTA-AMINOLEVULINIC ACID DEHYDRATASE; 1.
DR   Pfam; PF00490; ALAD; 1.
DR   PIRSF; PIRSF001415; Porphbilin_synth; 1.
DR   PRINTS; PR00144; DALDHYDRTASE.
DR   SMART; SM01004; ALAD; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00169; D_ALA_DEHYDRATASE; 1.
PE   3: Inferred from homology;
KW   Heme biosynthesis; Lyase; Magnesium; Metal-binding; Porphyrin biosynthesis;
KW   Zinc.
FT   CHAIN           1..324
FT                   /note="Delta-aminolevulinic acid dehydratase"
FT                   /id="PRO_0000140513"
FT   ACT_SITE        195
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        248
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         233
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         274
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         313
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
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
//