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Database: UniProt
Entry: A0A1C6NYN4_9BURK
LinkDB: A0A1C6NYN4_9BURK
Original site: A0A1C6NYN4_9BURK 
ID   A0A1C6NYN4_9BURK        Unreviewed;       334 AA.
AC   A0A1C6NYN4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=VAR608DRAFT_3299 {ECO:0000313|EMBL:SCK36142.1};
OS   Variovorax sp. HW608.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1034889 {ECO:0000313|EMBL:SCK36142.1, ECO:0000313|Proteomes:UP000198203};
RN   [1] {ECO:0000313|Proteomes:UP000198203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HW608 {ECO:0000313|Proteomes:UP000198203};
RA   Varghese N., Submissions Spin;
RL   Submitted (JUN-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; LT607803; SCK36142.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6NYN4; -.
DR   OrthoDB; 9805001at2; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000198203; Chromosome i.
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}.
FT   ACT_SITE        202
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         242
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ   SEQUENCE   334 AA;  36641 MW;  FB2CA02BEE26C0EB CRC64;
     MTLHAPFPAG RPRRLRRDAF TRDLVREHML STNDLIYPVF VQEGEKRRDP VPSMPGVERL
     SLDALLPVAE ECVELGITVM ALFPVIDPSL KTPAGDEACN PDGLIPRVVA SLKSRFPELG
     VMTDVALDPY TSHGQDGLLD ETGYILNDPT VEVLVKQALT QSRAGVDIVA PSDMMDGRIG
     AIRQALEARG DIHTRIMAYS AKYASAFYGP FRDAVGSAAN LGKSNKKVYQ MDPGNSNEAL
     REVAIDIAEG ADMVMVKPGM PYLDIVRRVK DEFQVPTFAY QVSGEYAMLM AAAQNGWLDR
     DAVILESLLA FKRAGADGVL TYFARDAARL LKRR
//
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