ID E0XWS0_9GAMM Unreviewed; 336 AA.
AC E0XWS0;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 03-MAY-2023, entry version 31.
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};
OS uncultured Pseudomonadales bacterium HF0010_05E14.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC environmental samples.
OX NCBI_TaxID=710778 {ECO:0000313|EMBL:ADI18861.1};
RN [1] {ECO:0000313|EMBL:ADI18861.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20695878; DOI=10.1111/j.1462-2920.2010.02314.x;
RA Rich V.I., Pham V.D., Eppley J., Shi Y., DeLong E.F.;
RT "Time-series analyses of Monterey Bay coastal microbial picoplankton using
RT a 'genome proxy' microarray.";
RL Environ. Microbiol. 13:116-134(2011).
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 Evidence={ECO:0000256|ARBA:ARBA00001227,
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}.
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DR EMBL; GU474902; ADI18861.1; -; Genomic_DNA.
DR AlphaFoldDB; E0XWS0; -.
DR UniPathway; UPA00251; UER00318.
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:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04823; ALAD_PBGS_aspartate_rich; 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 {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:PIRSR001415-5};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW ECO:0000256|RuleBase:RU000515}.
FT ACT_SITE 206
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 260
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ SEQUENCE 336 AA; 37567 MW; 74FBE1365EEA5B84 CRC64;
MKGSTKNRGQ FPYTRMRRNR KSSSIRKLVQ ESTLEITDLI QPVFVIDGNN KTESITSMPG
INRCSPDQLL NEAQELYNLG IQSIAIFPVI KKEKKSLNAE ESFNENGLVQ NTIKLLKRNI
PELTLITDVA LDPYTTHGHD GILNQKNIID NDLTNETLVK QALSHAVAGA DIIAPSDMMD
GRILRIREKL ESHNFHDTII MSYASKYASN YYGPFRDAIG SSDREKIDKS TYQIDIHNTD
EAISECELDL QEGADILLIK PGMPYLDIIT AVKQTFGVPT FAYQVSGEYS MHCLAFEKGL
LERDSTLLES LIAFKRAGAD AILTYFAKEA AILLNG
//
