ID   U7U8E2_9BURK            Unreviewed;       339 AA.
AC   U7U8E2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, 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};
GN   ORFNames=N879_20180 {ECO:0000313|EMBL:ERT55697.1};
OS   Alcaligenes sp. EGD-AK7.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Alcaligenes.
OX   NCBI_TaxID=1386079 {ECO:0000313|EMBL:ERT55697.1, ECO:0000313|Proteomes:UP000016497};
RN   [1] {ECO:0000313|EMBL:ERT55697.1, ECO:0000313|Proteomes:UP000016497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EGD-AK7 {ECO:0000313|EMBL:ERT55697.1};
RX   PubMed=24407646;
RA   Sagarkar S., Bhardwaj P., Yadav T.C., Qureshi A., Khardenavis A.,
RA   Purohit H.J., Kapley A.;
RT   "Draft genome sequence of atrazine-utilizing bacteria isolated from Indian
RT   agricultural soil.";
RL   Genome Announc. 2:e01149-13(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERT55697.1}.
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DR   EMBL; AVOG02000010; ERT55697.1; -; Genomic_DNA.
DR   RefSeq; WP_022983335.1; NZ_AVOG02000010.1.
DR   AlphaFoldDB; U7U8E2; -.
DR   OrthoDB; 9805001at2; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000016497; 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: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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016497}.
FT   ACT_SITE        205
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   339 AA;  37641 MW;  F322BAFFD7C58988 CRC64;
     MTRFIPPADF PNTRLRRNRR DEFSRRLVRE NRLSTDDLIY PVFVREGERV QEQVGSMPGV
     MRYSPDELMR VAEQCLELGI PVLSLFPSID PSLKTPDGSE AANPNGLIPR VVGMLKQQFP
     ELGVLTDVAL DPYTSHGQDG ILDEAGHILN EETVAMLIRQ AQTQAQAGVD IVAPSDMMDG
     RIGSIRAALD KDQFIHTRIM AYSAKYASAF YGPFRDAVGS AANLGRSNKN TYQMDPANRN
     EALREVAADI REGADMVMVK PGLPYLDILR DVKDAFGMPT YAYQVSGEYA MIKAAAQNGW
     LDHDKVMMES LLAFKRAGGD GILTYFAIEA AKLMREQNC
//