ID A0A0H4KNS6_9BACI Unreviewed; 323 AA.
AC A0A0H4KNS6; A0A231SL72;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|ARBA:ARBA00020771};
DE EC=4.2.1.24 {ECO:0000256|ARBA:ARBA00012053};
DE AltName: Full=Porphobilinogen synthase {ECO:0000256|ARBA:ARBA00032837};
GN ORFNames=B1B01_01260 {ECO:0000313|EMBL:OXS72104.1}, BEH_20695
GN {ECO:0000313|EMBL:AKO95180.1};
OS Priestia filamentosa.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=1402861 {ECO:0000313|EMBL:AKO95180.1, ECO:0000313|Proteomes:UP000036202};
RN [1] {ECO:0000313|EMBL:AKO95180.1, ECO:0000313|Proteomes:UP000036202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hbe603 {ECO:0000313|EMBL:AKO95180.1,
RC ECO:0000313|Proteomes:UP000036202};
RX PubMed=26248285;
RA Jia N., Du J., Ding M.Z., Gao F., Yuan Y.J.;
RT "Genome Sequence of Bacillus endophyticus and Analysis of Its Companion
RT Mechanism in the Ketogulonigenium vulgare-Bacillus Strain Consortium.";
RL PLoS ONE 10:E0135104-E0135104(2015).
RN [2] {ECO:0000313|Proteomes:UP000036202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hbe603 {ECO:0000313|Proteomes:UP000036202};
RA Jia N., Du J., Ding M.-Z., Gao F., Yuan Y.-J.;
RT "Genome Sequence of Bacillus endophyticus and Analysis of its Companion
RT Mechanism in the Ketogulonigenium vulgare-Bacillus strain Consortium.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AKO95180.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hbe603 {ECO:0000313|EMBL:AKO95180.1};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000215399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27955 {ECO:0000313|Proteomes:UP000215399};
RA Dastager S.G., Neurgaonkar P.S., Dharne M.S.;
RT "Bacillus sp. V-88(T) DSM27956, whole genome shotgun sequencing project.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:OXS72104.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 27955 {ECO:0000313|EMBL:OXS72104.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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 -!- 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 -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000256|ARBA:ARBA00008055,
CC ECO:0000256|RuleBase:RU004161}.
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DR EMBL; CP011974; AKO95180.1; -; Genomic_DNA.
DR EMBL; MWSI01000001; OXS72104.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H4KNS6; -.
DR KEGG; beo:BEH_20695; -.
DR PATRIC; fig|135735.6.peg.4381; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000036202; Chromosome.
DR Proteomes; UP000215399; 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; cd00384; ALAD_PBGS; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR001731; ALAD.
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.
PE 3: Inferred from homology;
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001415-5};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001415-3};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000036202};
KW Zinc {ECO:0000256|PIRSR:PIRSR001415-3}.
FT ACT_SITE 192
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 245
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT BINDING 202
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
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 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
FT BINDING 271
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 310
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
SQ SEQUENCE 323 AA; 36262 MW; 78FC8A097B03FF2F CRC64;
MFDRHRRLRS SENMRALVRE NHLRPEDFIY PIFVVEGENI RSEVSSMPDV YHVSLDYLNK
EIEELVELGV LSVMVFGVPA HKDEVGSQAY DEHGIVQKAI SQIKENFPEM VVIADTCLCQ
YTDHGHCGVI EGGKILNDPT LDLLARTAVS QAKAGADIIA PSNMMDGFVA AIRHGLDEEG
FEDVPIMSYA VKYSSAFYGP FRDAAHSTPQ FGDRKTYQMD PANRTEAIRE AQSDVDEDAD
FLIVKPALSY LDIVRDVRDR FNVPVVAYNV SGEYSMVKAA AANGWVNERD IVLEKLISMK
RAGADLIVTY HAKDASRWLR EKN
//
