HEM2_STRCO
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 03-AUG-2022, entry version 116.
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; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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}.
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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.SCO3311; -.
DR ChEMBL; CHEMBL3308959; -.
DR GeneID; 1098745; -.
DR KEGG; sco:SCO3311; -.
DR PATRIC; fig|100226.15.peg.3371; -.
DR eggNOG; COG0113; Bacteria.
DR HOGENOM; CLU_035731_0_0_11; -.
DR InParanoid; P54919; -.
DR OMA; YQMDYAN; -.
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 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;
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
