ID   HEM2_RHOCA              Reviewed;         332 AA.
AC   P42504;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 83.
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;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PAS100;
RX   PubMed=7784513; DOI=10.1104/pp.108.1.421;
RA   Indest K., Biel A.J.;
RT   "Nucleotide sequence of the Rhodobacter capsulatus hemB gene.";
RL   Plant Physiol. 108:421-421(1995).
RN   [2]
RP   CATALYTIC ACTIVITY, FUNCTION, AND SUBUNIT.
RX   PubMed=15555082; DOI=10.1186/1471-2091-5-17;
RA   Bollivar D.W., Clauson C., Lighthall R., Forbes S., Kokona B., Fairman R.,
RA   Kundrat L., Jaffe E.K.;
RT   "Rhodobacter capsulatus porphobilinogen synthase, a high activity metal ion
RT   independent hexamer.";
RL   BMC Biochem. 5:17-17(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
CC       porphobilinogen. {ECO:0000269|PubMed:15555082}.
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:0000269|PubMed:15555082};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:15555082}.
CC   -!- MISCELLANEOUS: Does not seem to have a metal requirement for activity.
CC       {ECO:0000269|PubMed:15555082}.
CC   -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000305}.
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DR   EMBL; U14593; AAA92884.1; -; Genomic_DNA.
DR   AlphaFoldDB; P42504; -.
DR   SMR; P42504; -.
DR   BioCyc; MetaCyc:MON-13250; -.
DR   UniPathway; UPA00251; UER00318.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004655; F:porphobilinogen synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
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   1: Evidence at protein level;
KW   Heme biosynthesis; Lyase; Porphyrin biosynthesis.
FT   CHAIN           1..332
FT                   /note="Delta-aminolevulinic acid dehydratase"
FT                   /id="PRO_0000140508"
FT   ACT_SITE        202
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        256
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         282
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         321
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   332 AA;  35854 MW;  4118DED5A15C8DBE CRC64;
     MTLITPPFPT NRLRRMRRTE ALRDLAQENR LSVKDLIWPI FITDVPGADV EISSMPGVVR
     RTMDGALKAA EGSRDAGHSR DLPVPLTDPA VKTETCEMAW QPDNFTNRVI AAMKQAVPEV
     AIMTDIALDP YNANGHDGLV RDGILLNDET TEALVKMALA QAAAGADILG PSDMMDGRVG
     AIRQAMEAAG HKDIAILSYA AKYASAFYGP FRDAVGASSA LKGDKKTYQM NPANSAEALR
     NVARDIAEGA DMVMVKPGMP YLDIVRQVKD AFGMPTYAYQ VSGEYAMLMA AVQNGWLNHD
     KVMLESLMAF RRAGCDGVLT YFAPAAAKLI GA