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Database: UniProt
Entry: A0A1P8FGH3_9PROT
LinkDB: A0A1P8FGH3_9PROT
Original site: A0A1P8FGH3_9PROT 
ID   A0A1P8FGH3_9PROT        Unreviewed;       324 AA.
AC   A0A1P8FGH3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=BWI17_05145 {ECO:0000313|EMBL:APV49118.1};
OS   Betaproteobacteria bacterium GR16-43.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1904640 {ECO:0000313|EMBL:APV49118.1, ECO:0000313|Proteomes:UP000185830};
RN   [1] {ECO:0000313|EMBL:APV49118.1, ECO:0000313|Proteomes:UP000185830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GR16-43 {ECO:0000313|EMBL:APV49118.1,
RC   ECO:0000313|Proteomes:UP000185830};
RA   Choi A.;
RT   "Complete genome sequence of betaproteobacterium GR16-43, isolated from a
RT   freshwater pond in South Korea.";
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; CP019169; APV49118.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1P8FGH3; -.
DR   STRING; 1904640.BWI17_05145; -.
DR   KEGG; beba:BWI17_05145; -.
DR   OrthoDB; 9805001at2; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000185830; 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   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        191
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   ACT_SITE        246
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   BINDING         231
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ   SEQUENCE   324 AA;  35055 MW;  CB9AAE706C7AF41D CRC64;
     MRRARRDDFS RRLVRENRLS ADNLILPVFV LDGAKKTEAV PSMPGVFRRT IDELIPVAEQ
     ALTLGIPALA LFPVIEPVLK TAGAEEAWNA NGLVPRTVRE LKKRFPQLGV ITDIALDPYT
     IHGQDGLIDA GGYVVNDETL AALSKQALAH AQAGVDIVAP SDMMDGRVGS LRHALDGAGF
     IHTRILAYSA KYASAFYGPF RDAVGSGASL GTGDKKTYQM DPGNTDEALH EVALDLEEGA
     DFVMVKPGMP YLDIVRRVKD RFGVPTFVYQ VSGEYAMLKA AAAQGWIDGE ACMMESLLGF
     RRAGADAILT YFAMDAAKIL KARA
//
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