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Entry: A0A171DD67_9ACTN
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ID   A0A171DD67_9ACTN        Unreviewed;       328 AA.
AC   A0A171DD67;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=PS9374_03693 {ECO:0000313|EMBL:GAT68032.1};
OS   Planomonospora sphaerica.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Planomonospora.
OX   NCBI_TaxID=161355 {ECO:0000313|EMBL:GAT68032.1, ECO:0000313|Proteomes:UP000077701};
RN   [1] {ECO:0000313|EMBL:GAT68032.1, ECO:0000313|Proteomes:UP000077701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 9374 {ECO:0000313|EMBL:GAT68032.1,
RC   ECO:0000313|Proteomes:UP000077701};
RA   Dohra H., Suzuki T., Inoue Y., Kodani S.;
RT   "Draft Genome Sequence of Planomonospora sphaerica JCM9374, a Rare
RT   Actinomycete.";
RL   Genome Announc. 4:e00779-16(2016).
RN   [2] {ECO:0000313|Proteomes:UP000077701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 9374 {ECO:0000313|Proteomes:UP000077701};
RA   Suzuki T., Dohra H., Kodani S.;
RT   "Planomonospora sphaerica JCM9374 whole genome shotgun sequence.";
RL   Submitted (APR-2016) 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: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:GAT68032.1}.
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DR   EMBL; BDCX01000008; GAT68032.1; -; Genomic_DNA.
DR   RefSeq; WP_068898173.1; NZ_BDCX01000008.1.
DR   AlphaFoldDB; A0A171DD67; -.
DR   STRING; 161355.PS9374_03693; -.
DR   OrthoDB; 9805001at2; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000077701; 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; 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 {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:UP000077701}.
FT   ACT_SITE        199
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   ACT_SITE        253
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   BINDING         209
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT   BINDING         221
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT   BINDING         238
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
FT   BINDING         279
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT   BINDING         318
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
SQ   SEQUENCE   328 AA;  35037 MW;  60F562AD92DB7665 CRC64;
     MTAQFPAARP RRLRRTSPMR RMVAGTRLHP AELVLPMFVK EGIDEPNPIG SMPGVFQHTR
     DSLRKAAHEA AEAGVGGLIL FGIPAVKDAR GSAGDDPDGI VQQGVADLVA EVGDAMVVMT
     DTCLDEFTDH GHCGVLTAGG EVDNDATLER YAAVAVAQAR AGSQVIAPSG MMDGQVAAIR
     AALDAEGFEQ VPILAYSAKY ASAFYGPFRE AAECAPQFGD RNAYQQDPAG PVGEALREVR
     LDLAEGADAV MVKPALLYLD ILRQVRDEVD VPVAAYQISG EYAMIEAAAA NGWIDRDRAI
     MESLVAIRRA GADMILTYWA TEAARRLR
//
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