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Database: UniProt
Entry: J3JG75_9EURY
LinkDB: J3JG75_9EURY
Original site: J3JG75_9EURY 
ID   J3JG75_9EURY            Unreviewed;       326 AA.
AC   J3JG75;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515};
DE            EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515};
GN   ORFNames=HSB1_20090 {ECO:0000313|EMBL:EJN59851.1};
OS   Halogranum salarium B-1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae.
OX   NCBI_TaxID=1210908 {ECO:0000313|EMBL:EJN59851.1, ECO:0000313|Proteomes:UP000007813};
RN   [1] {ECO:0000313|EMBL:EJN59851.1, ECO:0000313|Proteomes:UP000007813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-1 {ECO:0000313|EMBL:EJN59851.1,
RC   ECO:0000313|Proteomes:UP000007813};
RX   PubMed=23144405; DOI=10.1128/JB.01815-12;
RA   Kim K.K., Lee K.C., Lee J.S.;
RT   "Draft Genome Sequence of the Extremely Halophilic Archaeon Halogranum
RT   salarium B-1T.";
RL   J. Bacteriol. 194:6659-6659(2012).
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:EJN59851.1}.
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DR   EMBL; ALJD01000004; EJN59851.1; -; Genomic_DNA.
DR   RefSeq; WP_009367090.1; NZ_ALJD01000004.1.
DR   AlphaFoldDB; J3JG75; -.
DR   PATRIC; fig|1210908.3.peg.1926; -.
DR   eggNOG; arCOG04300; Archaea.
DR   OrthoDB; 8493at2157; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000007813; 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:PIRSR001415-3};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW   ECO:0000256|RuleBase:RU000515}; Zinc {ECO:0000256|PIRSR:PIRSR001415-3}.
FT   ACT_SITE        199
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   ACT_SITE        252
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT   BINDING         127
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
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         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
FT   BINDING         278
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT   BINDING         317
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
SQ   SEQUENCE   326 AA;  35849 MW;  115416672AB4796C CRC64;
     MNLRDRPRRL RTDGVRPLVS ETRLDATDLI APVFVDATTD ERVPIETMPG HERVPVDEAV
     ARVEEIRETG VEAVMLFGIP NAKDEYGSRA WAEDGVVQEA TRRVKAETDT YVITDVCLCE
     YTSHGHCGLV EPEAEENPRL TVQNDETLDL LAKTAVSHAD AGADMVAPSA MTDGMVRAIR
     EGLDESGFSD VPIMSYAAKY ESAFYGPFRD AADGAPAFGD RRHYQMDPAN AREAMREVKL
     DVEEGADVLM VKPALPYLDI VRDVREAFDH PVAAYNVSGE YAMLHAAADK GWLNLEETAV
     ESLLSIKRAG ADLILTYFAE DVAESL
//
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