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Database: UniProt
Entry: A0A1P8U7A1_9MICO
LinkDB: A0A1P8U7A1_9MICO
Original site: A0A1P8U7A1_9MICO 
ID   A0A1P8U7A1_9MICO        Unreviewed;       331 AA.
AC   A0A1P8U7A1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=BOH66_06750 {ECO:0000313|EMBL:APZ33991.1};
OS   Microbacterium aurum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=36805 {ECO:0000313|EMBL:APZ33991.1, ECO:0000313|Proteomes:UP000187185};
RN   [1] {ECO:0000313|EMBL:APZ33991.1, ECO:0000313|Proteomes:UP000187185}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KACC 15219 {ECO:0000313|EMBL:APZ33991.1,
RC   ECO:0000313|Proteomes:UP000187185};
RA   Jung Y., Shin J.-H., Lee Y.-J., Yi H., Bahn Y.-S., Kim J.F., Lee D.-W.;
RT   "Complete genome sequence of Microbacterium aurum KACC 15219.";
RL   Submitted (DEC-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}.
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DR   EMBL; CP018762; APZ33991.1; -; Genomic_DNA.
DR   RefSeq; WP_076690307.1; NZ_JAFBCQ010000001.1.
DR   AlphaFoldDB; A0A1P8U7A1; -.
DR   STRING; 36805.BOH66_06750; -.
DR   KEGG; maur:BOH66_06750; -.
DR   OrthoDB; 9805001at2; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000187185; Chromosome.
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   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:UP000187185}.
FT   ACT_SITE        198
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   ACT_SITE        250
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   BINDING         208
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT   BINDING         219
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT   BINDING         235
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
FT   BINDING         276
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT   BINDING         315
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
SQ   SEQUENCE   331 AA;  34749 MW;  93183631B5D1D5E9 CRC64;
     MTAYPVRRLR RLRHSPALRR LVAETRLHPA QLVLPVFVKE DIDAPQPIAS MPGVSQHPLH
     GLPAVVEEAA AAGIGGIMLF GVPTHRDAVG SGAIDPDGIL NRAIRVAAEA AAGRLTVQAD
     LCLDEFTDHG HCGVLAADGS VDNDATLEVY ARMALAQADA GAAILGLSGM MDGQVAACRA
     ALDAAGRTDV VLLAYSAKYA SAFYGPFRDA VESTLQGDRR TYQLDPGNGR EGVQEALADV
     DEGADIVMVK PAGPYLDVLA EVAAVSPVPV WAYQVSGEYA MIEHAAASGV IDRERAIGES
     LVGIRRAGAE AILTYWAIEV AGWLRDGRSL A
//
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