ID A1AL55_PELPD Unreviewed; 325 AA. AC A1AL55; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 02-SEP-2026, entry version 97. DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|ARBA:ARBA00020771, ECO:0000256|RuleBase:RU000515}; DE EC=4.2.1.24 {ECO:0000256|ARBA:ARBA00012053, ECO:0000256|RuleBase:RU000515}; GN OrderedLocusNames=Ppro_0442 {ECO:0000313|EMBL:ABK98075.1}; OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1). OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfuromonadia; OC Desulfuromonadales; Desulfuromonadaceae; Pelobacter. OX NCBI_TaxID=338966 {ECO:0000313|EMBL:ABK98075.1, ECO:0000313|Proteomes:UP000006732}; RN [1] {ECO:0000313|EMBL:ABK98075.1, ECO:0000313|Proteomes:UP000006732} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1 RC {ECO:0000313|Proteomes:UP000006732}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D., RA Richardson P.; RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379."; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 5-aminolevulinate = porphobilinogen + 2 H2O + H(+); 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:0000256|ARBA:ARBA00047651, CC ECO:0000256|RuleBase:RU000515}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. CC {ECO:0000256|ARBA:ARBA00004694}. CC -!- SUBUNIT: Homooctamer. {ECO:0000256|RuleBase:RU000515}. CC -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000256|ARBA:ARBA00008055, CC ECO:0000256|RuleBase:RU004161}. 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; CP000482; ABK98075.1; -; Genomic_DNA. DR RefSeq; WP_011734389.1; NC_008609.1. DR AlphaFoldDB; A1AL55; -. DR STRING; 338966.Ppro_0442; -. DR KEGG; ppd:Ppro_0442; -. DR eggNOG; COG0113; Bacteria. DR HOGENOM; CLU_035731_0_0_7; -. DR OrthoDB; 9805001at2; -. DR UniPathway; UPA00251; UER00318. DR Proteomes; UP000006732; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004655; F:porphobilinogen synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:TreeGrafter. DR GO; GO:0006783; P:heme biosynthetic process; IEA:TreeGrafter. DR CDD; cd00384; ALAD_PBGS; 1. DR FunFam; 3.20.20.70:FF:000019; Delta-aminolevulinic acid dehydratase; 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 NCBIfam; NF006762; PRK09283.1; 1. 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 {ECO:0000256|ARBA:ARBA00023133}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000515}; KW Magnesium {ECO:0000256|PIRSR:PIRSR001415-5}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001415-3}; KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, KW ECO:0000256|RuleBase:RU000515}; KW Reference proteome {ECO:0000313|Proteomes:UP000006732}; KW Zinc {ECO:0000256|PIRSR:PIRSR001415-3}. FT ACT_SITE 195 FT /note="Schiff-base intermediate with substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1" FT ACT_SITE 248 FT /note="Schiff-base intermediate with substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1" FT BINDING 120 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3" FT BINDING 122 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3" FT BINDING 130 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3" FT BINDING 205 FT /ligand="5-aminolevulinate" FT /ligand_id="ChEBI:CHEBI:356416" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2" FT BINDING 217 FT /ligand="5-aminolevulinate" FT /ligand_id="ChEBI:CHEBI:356416" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2" FT BINDING 233 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5" FT BINDING 274 FT /ligand="5-aminolevulinate" FT /ligand_id="ChEBI:CHEBI:356416" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2" FT BINDING 313 FT /ligand="5-aminolevulinate" FT /ligand_id="ChEBI:CHEBI:356416" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2" SQ SEQUENCE 325 AA; 35824 MW; 0FA86AA1A4C20A9F CRC64; MRESYFRARR IRGNETMRRM VRETSLSVDD LVYPLFSAFG SGIMKEISSM PGIYQQSIEH LVEECREVQG LGIPAVLLFG IPESKDGVGS DAYSDSGIIQ ETIRAIKREV PGLTVITDVC LCEYTDHGHC GVIEDGDVDN DATLELLAKE ALSHVRAGAD MVAPSDMMDG RVAAIREALD NSGFSSVPVM SYAVKYASGY YGPFREAAES TPQFGDRRSY QMDPANRREA LREASADIDE GADIIMVKPG LPYLDILRDL RNSCNLPLAV YNVSGEYSMV KAAAANGWID EERVVLETML GFKRAGADII ITYHAKDVAR WLGRN //