ID HEM2_HELPY Reviewed; 323 AA. AC P56074; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 121. 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=HP_0163; OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85962; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). 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; AE000511; AAD07232.1; -; Genomic_DNA. DR PIR; C64540; C64540. DR RefSeq; NP_206962.1; NC_000915.1. DR RefSeq; WP_000476591.1; NC_018939.1. DR AlphaFoldDB; P56074; -. DR SMR; P56074; -. DR IntAct; P56074; 1. DR STRING; 85962.HP_0163; -. DR PaxDb; 85962-C694_00810; -. DR EnsemblBacteria; AAD07232; AAD07232; HP_0163. DR KEGG; hpy:HP_0163; -. DR PATRIC; fig|85962.47.peg.176; -. DR eggNOG; COG0113; Bacteria. DR InParanoid; P56074; -. DR OrthoDB; 9805001at2; -. DR PhylomeDB; P56074; -. DR UniPathway; UPA00251; UER00318. DR Proteomes; UP000000429; 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; Zinc. FT CHAIN 1..323 FT /note="Delta-aminolevulinic acid dehydratase" FT /id="PRO_0000140502" FT ACT_SITE 193 FT /note="Schiff-base intermediate with substrate" FT /evidence="ECO:0000250" FT ACT_SITE 246 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 203 FT /ligand="5-aminolevulinate" FT /ligand_id="ChEBI:CHEBI:356416" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 215 FT /ligand="5-aminolevulinate" FT /ligand_id="ChEBI:CHEBI:356416" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 231 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 272 FT /ligand="5-aminolevulinate" FT /ligand_id="ChEBI:CHEBI:356416" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 311 FT /ligand="5-aminolevulinate" FT /ligand_id="ChEBI:CHEBI:356416" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 323 AA; 36203 MW; ADB784A450856CA2 CRC64; MFKRLRRLRS SENLRAMLRE TRLNIDDFIA PLFVIESDSC IKNEISSMPG VYQMSMEPLL KECEELVGLG VKAVLLFGIP KHKDATGSHA LNKDHIVAKA AKEIKKRFKD LIVIADLCFC EYTDHGHCGI LENASVSNDK TLEILNLQGL ILAESGVDIL APSNMMDGNV LSLRKTLDNA GYTHTPIMSY STKFASSYYG PFRDVANSAP SFGDRKSYQM DYANQKEALL ESLEDEKQGA DILMVKPALA YLDIVKEIRD HTLLPLALYN VSGEYAMLKL AQKHNLINYE SVLLETMTCF KRAGADMIIS YHAKEVANLL QRN //