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Database: UniProt
Entry: A0A0U3E9J4_9CREN
LinkDB: A0A0U3E9J4_9CREN
Original site: A0A0U3E9J4_9CREN 
ID   A0A0U3E9J4_9CREN        Unreviewed;       341 AA.
AC   A0A0U3E9J4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515};
DE            EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515};
GN   ORFNames=EYM_06895 {ECO:0000313|EMBL:ALU11982.1};
OS   Ignicoccus islandicus DSM 13165.
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignicoccus.
OX   NCBI_TaxID=940295 {ECO:0000313|EMBL:ALU11982.1, ECO:0000313|Proteomes:UP000060778};
RN   [1] {ECO:0000313|EMBL:ALU11982.1, ECO:0000313|Proteomes:UP000060778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13165 {ECO:0000313|EMBL:ALU11982.1,
RC   ECO:0000313|Proteomes:UP000060778};
RA   Podar M.;
RT   "Comparative genomics of Ignicoccus.";
RL   Submitted (NOV-2013) 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; CP006867; ALU11982.1; -; Genomic_DNA.
DR   RefSeq; WP_075050318.1; NZ_CP006867.1.
DR   AlphaFoldDB; A0A0U3E9J4; -.
DR   STRING; 940295.EYM_06895; -.
DR   GeneID; 30680752; -.
DR   KEGG; iis:EYM_06895; -.
DR   PATRIC; fig|940295.4.peg.1340; -.
DR   OrthoDB; 8493at2157; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000060778; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000060778};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001415-3}.
FT   ACT_SITE        204
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   ACT_SITE        257
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   BINDING         121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT   BINDING         123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT   BINDING         214
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT   BINDING         226
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT   BINDING         242
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
FT   BINDING         284
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT   BINDING         323
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
SQ   SEQUENCE   341 AA;  38072 MW;  6C14C3664CF59D86 CRC64;
     MSFPYLRPRR LRKNLYLRDL VAETRVSPRD FIFPIFVKEG ISEPEPINSM PGQYRWPVEK
     VTKIVSDALE LGVRNVLIFG IPSYKDELGS SAYSKDGVVQ RAVKKIRKEF GDEVVIHTDV
     CLCHYTTHGH CGLLTRKCVG DFCRDVIDND STIELLGKVA VTHAEAGADV VAPSSMMDGM
     VRTIRKALDE AGFTDVAIMS YAAKYASAFY GPFREAADNA PQKGDRRTYQ MDPRNGEEAI
     KEVALDVEEG ADILMVKPAL AYLDVIRRVR EAFPHYPLAA YNVSGEYSMV KVAAANGLVD
     EKKIILEILH AIKRAGANVI ITYHALEAAQ WLKEGLDREL F
//
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