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Database: UniProt
Entry: A0A1Y2BPI1_9FUNG
LinkDB: A0A1Y2BPI1_9FUNG
Original site: A0A1Y2BPI1_9FUNG 
ID   A0A1Y2BPI1_9FUNG        Unreviewed;       293 AA.
AC   A0A1Y2BPI1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   22-FEB-2023, entry version 20.
DE   RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515};
DE            EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515};
GN   ORFNames=BCR33DRAFT_721866 {ECO:0000313|EMBL:ORY36646.1};
OS   Rhizoclosmatium globosum.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Chytridiales;
OC   Chytriomycetaceae; Rhizoclosmatium.
OX   NCBI_TaxID=329046 {ECO:0000313|EMBL:ORY36646.1, ECO:0000313|Proteomes:UP000193642};
RN   [1] {ECO:0000313|EMBL:ORY36646.1, ECO:0000313|Proteomes:UP000193642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEL800 {ECO:0000313|EMBL:ORY36646.1,
RC   ECO:0000313|Proteomes:UP000193642};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles.
CC       Binds two molecules of 5-aminolevulinate per subunit, each at a
CC       distinct site, and catalyzes their condensation to form
CC       porphobilinogen. {ECO:0000256|ARBA:ARBA00025628}.
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:ORY36646.1}.
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DR   EMBL; MCGO01000054; ORY36646.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2BPI1; -.
DR   STRING; 329046.A0A1Y2BPI1; -.
DR   OrthoDB; 2782182at2759; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000193642; 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   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   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:UP000193642};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR001415-3}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..293
FT                   /note="Delta-aminolevulinic acid dehydratase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012305158"
FT   ACT_SITE        155
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   ACT_SITE        208
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT   BINDING         165
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT   BINDING         177
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT   BINDING         235
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT   BINDING         274
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
SQ   SEQUENCE   293 AA;  31558 MW;  DE211B4CA9681258 CRC64;
     MPGVSRFGVN RLAAFLSPLV LNGLKSVLLF GVPNDNDNDG IKKDASASAA DDDSGPVISA
     IKLIRTCFPD LLVACDVCLC PYSDHGHCGV LNQDGSINNP LSIARLAQIS LKYAQAGCHV
     IAPSDMMDGR IGAIKDILRL NGLNGNVAVL AYSAKFASGF YGPFRDAACS SPASGDRKRY
     QLPPNSRALA RRANARDAQE GADMLMVKPG YPYLDLVRDT REAHPDLPLA VYQVSGEYAM
     LWHAAQNKVF DLKVGVMEAT EACLRAGASI VITYYTPQIL EWLLQKESRA SKL
//
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