ID A0A0P9ISX9_PSESX Unreviewed; 336 AA. AC A0A0P9ISX9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-DEC-2018, entry version 8. DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515}; DE EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515}; GN ORFNames=ALO42_00608 {ECO:0000313|EMBL:KPW12792.1}; OS Pseudomonas syringae pv. atrofaciens. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=192087 {ECO:0000313|EMBL:KPW12792.1, ECO:0000313|Proteomes:UP000050311}; RN [1] {ECO:0000313|EMBL:KPW12792.1, ECO:0000313|Proteomes:UP000050311} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ICMP4394 {ECO:0000313|EMBL:KPW12792.1, RC ECO:0000313|Proteomes:UP000050311}; RA Thakur S., Wang P.W., Gong Y., Weir B.S., Guttman D.S.; RT "Genome announcement of multiple Pseudomonas syringae strains."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. 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:356416, ChEBI:CHEBI:58126; EC=4.2.1.24; CC Evidence={ECO:0000256|RuleBase:RU000515}; CC -!- SUBUNIT: Homooctamer. {ECO:0000256|RuleBase:RU000515}. CC -!- SIMILARITY: Belongs to the ALAD family. CC {ECO:0000256|RuleBase:RU004161}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPW12792.1}. 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; LJPO01000058; KPW12792.1; -; Genomic_DNA. DR RefSeq; WP_003317357.1; NZ_LJPO01000058.1. DR EnsemblBacteria; KPW12792; KPW12792; ALO42_00608. DR PATRIC; fig|192087.3.peg.815; -. DR Proteomes; UP000050311; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004655; F:porphobilinogen synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW. 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 Complete proteome {ECO:0000313|Proteomes:UP000050311}; KW Lyase {ECO:0000256|RuleBase:RU000515}; KW Magnesium {ECO:0000256|PIRSR:PIRSR001415-5}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001415-5}; KW Porphyrin biosynthesis {ECO:0000256|RuleBase:RU000515}. FT ACT_SITE 205 205 Schiff-base intermediate with substrate. FT {ECO:0000256|PIRSR:PIRSR001415-1}. FT ACT_SITE 260 260 Schiff-base intermediate with substrate. FT {ECO:0000256|PIRSR:PIRSR001415-1}. FT METAL 245 245 Magnesium. {ECO:0000256|PIRSR: FT PIRSR001415-5}. SQ SEQUENCE 336 AA; 36921 MW; E449956AFD692E0F CRC64; MSFTPANRLF PLTRLRRNRR DDFSRRLVRE NVVTVDDLIL PVFVLDGENR RESIASMPGV ERLSVDLLLK EAEHWVALGI PALALFPVTP PEKKSLDGAE AWNPDGIAQR ATRALRDRFP ELGVITDVAL DPFTTHGQDG ILDEEGYVQN DITVDALVKQ ALSHADAGAQ VVAPSDMMDG RIQAIRESLE LAGHVNVRIM AYSAKYASAY YGPFRDAVGS SLNLGKANKA SYQMDPANSN EALHEVAADL AEGADMVMVK PGMPYLDILY RVKDEFKVPT FVYQVSGEYA MHMAAIQNGW LSEGVILESL TAFKRAGADG ILTYFAVRAA QLLKGQ //