ID A0A0Q0T2Q7_9PSED Unreviewed; 324 AA.
AC A0A0Q0T2Q7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=AQS70_02200 {ECO:0000313|EMBL:KQB53584.1};
OS Pseudomonas endophytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1563157 {ECO:0000313|EMBL:KQB53584.1, ECO:0000313|Proteomes:UP000050342};
RN [1] {ECO:0000313|EMBL:KQB53584.1, ECO:0000313|Proteomes:UP000050342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSTT44 {ECO:0000313|EMBL:KQB53584.1,
RC ECO:0000313|Proteomes:UP000050342};
RA Von Neubeck M., Huptas C., Wenning M., Scherer S.;
RT "Pseudomonas helleri sp. nov. and Pseudomonas weihenstephanensis sp. nov.,
RT isolated from raw cows milk.";
RL Submitted (OCT-2015) 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}.
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:KQB53584.1}.
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DR EMBL; LLWH01000165; KQB53584.1; -; Genomic_DNA.
DR RefSeq; WP_055102993.1; NZ_LLWH01000165.1.
DR AlphaFoldDB; A0A0Q0T2Q7; -.
DR STRING; 1563157.AQS70_02200; -.
DR OrthoDB; 9805001at2; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000050342; 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; IPR030656; ALAD_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR PANTHER; PTHR11458; DELTA-AMINOLEVULINIC ACID DEHYDRATASE; 1.
DR PANTHER; PTHR11458:SF1; 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}; Zinc {ECO:0000256|PIRSR:PIRSR001415-3}.
FT ACT_SITE 197
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 249
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
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 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT BINDING 207
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 218
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
FT BINDING 275
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 314
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
SQ SEQUENCE 324 AA; 35359 MW; 38ECF1E5560DA407 CRC64;
MPNQFPSVRP RRLRRNQTLR DMFQETEFSL NDLVLPIFVE EDIDDFVPIT SMPGVMRIPE
SKLAGEIERY ARAGIKSVMA FGVSHHLDAT GSDSWREDGL VSRMARICKD TAPDMIVMSD
TCFCEYTSHG HCGVMHDHGV DNDATLINLG KQAVAAAAAG ADFISPSAAM DGQVQAIRSA
LDAAGFIDTS IMAYSTKFAS ALYGPFREAG GSALKGDRKS YQMNPMNRRE AIRESLLDEQ
EGADVLMVKP AGAYLDIIRD VREASRLPLA AYQVSGEYAM IKFGAQAGAI DEARVVRETL
GSIKRAGADM ILTYFAMDLA LQGI
//
