ID HEM2_STRCO Reviewed; 330 AA. AC P54919; Q9S2E6; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 27-MAR-2024, entry version 124. 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=SCO3311; ORFNames=SCE68.09c; OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145). OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group. OX NCBI_TaxID=100226; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=A3(2) / NRRL B-16638; RA Petricek M.; RT "Cloning and characterisation of the genes that encode enzymes for first RT steps of tetrapyrrole biosynthesis in Streptomyces coelicolor A3(2)."; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145; RX PubMed=12000953; DOI=10.1038/417141a; RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H., RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.; RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor RT A3(2)."; RL Nature 417:141-147(2002). 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 -!- 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; U19249; AAA61398.1; -; Genomic_DNA. DR EMBL; AL939116; CAB45345.1; -; Genomic_DNA. DR PIR; T36259; T36259. DR RefSeq; NP_627521.1; NC_003888.3. DR RefSeq; WP_011028903.1; NZ_VNID01000025.1. DR AlphaFoldDB; P54919; -. DR SMR; P54919; -. DR STRING; 100226.gene:17760930; -. DR ChEMBL; CHEMBL3308959; -. DR PaxDb; 100226-SCO3311; -. DR PATRIC; fig|100226.15.peg.3371; -. DR eggNOG; COG0113; Bacteria. DR HOGENOM; CLU_035731_0_0_11; -. DR InParanoid; P54919; -. DR OrthoDB; 9805001at2; -. DR PhylomeDB; P54919; -. DR UniPathway; UPA00251; UER00318. DR Proteomes; UP000001973; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004655; F:porphobilinogen synthase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central. 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 Reference proteome. FT CHAIN 1..330 FT /note="Delta-aminolevulinic acid dehydratase" FT /id="PRO_0000140519" FT ACT_SITE 203 FT /note="Schiff-base intermediate with substrate" FT /evidence="ECO:0000250" FT ACT_SITE 255 FT /note="Schiff-base intermediate with substrate" FT /evidence="ECO:0000250" FT BINDING 213 FT /ligand="5-aminolevulinate" FT /ligand_id="ChEBI:CHEBI:356416" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 224 FT /ligand="5-aminolevulinate" FT /ligand_id="ChEBI:CHEBI:356416" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 240 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 281 FT /ligand="5-aminolevulinate" FT /ligand_id="ChEBI:CHEBI:356416" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 320 FT /ligand="5-aminolevulinate" FT /ligand_id="ChEBI:CHEBI:356416" FT /ligand_label="2" FT /evidence="ECO:0000250" FT CONFLICT 100 FT /note="D -> V (in Ref. 1; AAA61398)" FT /evidence="ECO:0000305" SQ SEQUENCE 330 AA; 35453 MW; D2AF1F8B971F30F5 CRC64; MTTYGSFPGA RPRRLRTTPV MRRMVAETRL HPADFILPAF VREGVSEPVP IAAMPGVVQH TRDTLKKAAA EAVEAGVSGI MLFGVPEDGK KDAAGTAGTD PDGILQVALR DVRAEVGDEL LVMSDLCLDE FTDHGHCGVL DGQGRVDNDA TLERYAEMAQ VQADAGAHVV GPSGMMDGQI GVIRDALDQI GREDVAILAY TAKYASAFYG PFREAVGSSL KGDRKTYQQD SANARESLRE LALDLEEGAD MVMVKPAGPY LDILAKVAEA SDVPVAAYQI SGEYSMIEAA AEKGWIDRDR AILESLTGIK RAGARNILTY WATEVARTLR //