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Database: UniProt
Entry: A6ELH9_9BACT
LinkDB: A6ELH9_9BACT
Original site: A6ELH9_9BACT 
ID   A6ELH9_9BACT            Unreviewed;       329 AA.
AC   A6ELH9;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   22-FEB-2023, entry version 55.
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=SCB49_06467 {ECO:0000313|EMBL:EDM45429.1};
OS   unidentified eubacterium SCB49.
OC   Bacteria; Bacteroidota; environmental samples.
OX   NCBI_TaxID=50743 {ECO:0000313|EMBL:EDM45429.1, ECO:0000313|Proteomes:UP000003659};
RN   [1] {ECO:0000313|EMBL:EDM45429.1, ECO:0000313|Proteomes:UP000003659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCB49 {ECO:0000313|EMBL:EDM45429.1,
RC   ECO:0000313|Proteomes:UP000003659};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) 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:EDM45429.1}.
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DR   EMBL; ABCO01000001; EDM45429.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ELH9; -.
DR   STRING; 50743.SCB49_06467; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000003659; 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:UP000003659}.
FT   ACT_SITE        196
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   ACT_SITE        254
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   BINDING         239
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ   SEQUENCE   329 AA;  36625 MW;  88E26A8EB6C36623 CRC64;
     MYPLKRNRRL RTTEAMRSLV RENTITANDF IVPVFVVEGN GVKDEIPSMP NYYRYSLDTL
     QDEIKELWSL GLKSVLLFVK VPENLKDNAG KEALNPDGLM QRAIKTVKNT CPEMIVMTDV
     ALDPYSQYGH DGIVANGEIV NDPTTTFLAN MALSHAQAGA DVIAPSDMMD GRILAMRSLL
     EEEGFYNTGI MSYSAKYASA FYGPFRDALD SAPVDLQDIP KDKKSYQMDP ANREEAIRET
     LMDIDEGADI VMVKPGLCYL DIVRDIRNVV DIPVAVYQVS GEYAMLKAAA EKGWLDHDAV
     MMEQILSIKR AGATLIASYF AKDVVKLLS
//
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