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Database: UniProt
Entry: A0A1G9R2R9_9GAMM
LinkDB: A0A1G9R2R9_9GAMM
Original site: A0A1G9R2R9_9GAMM 
ID   A0A1G9R2R9_9GAMM        Unreviewed;       335 AA.
AC   A0A1G9R2R9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=SAMN05661010_03566 {ECO:0000313|EMBL:SDM17410.1};
OS   Halomonas muralis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=119000 {ECO:0000313|EMBL:SDM17410.1, ECO:0000313|Proteomes:UP000198654};
RN   [1] {ECO:0000313|EMBL:SDM17410.1, ECO:0000313|Proteomes:UP000198654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14789 {ECO:0000313|EMBL:SDM17410.1,
RC   ECO:0000313|Proteomes:UP000198654};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FNGI01000013; SDM17410.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9R2R9; -.
DR   STRING; 119000.SAMN05661010_03566; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000198654; 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:UP000198654}.
FT   ACT_SITE        204
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   ACT_SITE        259
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   BINDING         244
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ   SEQUENCE   335 AA;  36772 MW;  BABD464FD874C8E2 CRC64;
     MNPLVSRQYP ATRMRRMRKD DFSRRLMRES TLTPADLILP VFVLDGERRR EAVPSMPGVE
     RLSLDLLIEQ AREVSALGIP ALALFPVVGG QHKSELAEEA YNAGGLVQRS VRALKDACPE
     LGIITDVALD PYTSHGQDGI LDAQGYVEND RTVETLLKQA LSHAEAGADV VAPSDMMDGR
     IGAIRAVLEQ EQLHNARIMA YSAKYASHYY GPFRDALGSA GNLGKADKTT YQMDPANSDE
     AVHEVALDLA EGADMVMVKP GMPYLDVVRR IKQELRVPTF AYQVSGEYAM HMAAFDNGWL
     DADSVIIESL TCFKRAGADG VLTYFAKRAA QLLNQ
//
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