ID A0A0D5NLL4_9BACL Unreviewed; 328 AA.
AC A0A0D5NLL4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=VN24_17670 {ECO:0000313|EMBL:AJY76050.1};
OS Paenibacillus beijingensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1126833 {ECO:0000313|EMBL:AJY76050.1, ECO:0000313|Proteomes:UP000032633};
RN [1] {ECO:0000313|EMBL:AJY76050.1, ECO:0000313|Proteomes:UP000032633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24997 {ECO:0000313|EMBL:AJY76050.1,
RC ECO:0000313|Proteomes:UP000032633};
RX PubMed=25937453; DOI=10.1016/j.jbiotec.2015.04.015;
RA Kwak Y., Shin J.H.;
RT "Complete genome sequence of Paenibacillus beijingensis 7188(T) (=DSM
RT 24997(T)), a novel rhizobacterium from jujube garden soil.";
RL J. Biotechnol. 206:75-76(2015).
RN [2] {ECO:0000313|Proteomes:UP000032633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24997 {ECO:0000313|Proteomes:UP000032633};
RA Kwak Y., Shin J.-H.;
RT "Genome sequence of Paenibacillus beijingensis strain DSM 24997T.";
RL Submitted (MAR-2015) 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|ARBA:ARBA00011823,
CC 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; CP011058; AJY76050.1; -; Genomic_DNA.
DR RefSeq; WP_045671478.1; NZ_CP011058.1.
DR AlphaFoldDB; A0A0D5NLL4; -.
DR STRING; 1126833.VN24_17670; -.
DR KEGG; pbj:VN24_17670; -.
DR PATRIC; fig|1126833.4.peg.3878; -.
DR HOGENOM; CLU_035731_0_0_9; -.
DR OrthoDB; 9805001at2; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000032633; 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:UP000032633};
KW Zinc {ECO:0000256|PIRSR:PIRSR001415-3}.
FT ACT_SITE 201
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 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT BINDING 211
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 223
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
FT BINDING 280
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 319
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
SQ SEQUENCE 328 AA; 36160 MW; 4DA226F157E83980 CRC64;
MNFPTVRHRR LRRTAALRGL VRETVLTLND LIYPIYVTYG SDIKDEISSM PGVYRFSLDR
LEAEIREIVD AGITSIMIFG IPEHKDAVGT SAYDPNGIVQ EATRKVKEWA PDLVVIADTC
LCQYTDHGHC GIVHRNERTG EAEVDNDASL ALLVRTAVSQ AQAGADMIAP SNMMDGFVLS
IRAGLDEAGF ADIPILSYSV KYSSAYYGPF REAAHSAPQY GDRKSYQMDP ANLREALREA
ESDIAEGADM LMVKPALAYL DVIRALKENF DLPVAAYNVS GEYAMVKAAS ANGWIDEKSI
VMESLLGMKR AGADLIITYH AKDVARWL
//
