ID A0A1I7ET35_9FLAO Unreviewed; 331 AA.
AC A0A1I7ET35;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN05216480_10159 {ECO:0000313|EMBL:SFU27075.1};
OS Pustulibacterium marinum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Pustulibacterium.
OX NCBI_TaxID=1224947 {ECO:0000313|EMBL:SFU27075.1, ECO:0000313|Proteomes:UP000199138};
RN [1] {ECO:0000313|EMBL:SFU27075.1, ECO:0000313|Proteomes:UP000199138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12333 {ECO:0000313|EMBL:SFU27075.1,
RC ECO:0000313|Proteomes:UP000199138};
RA de Groot N.N.;
RL Submitted (OCT-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; FPBK01000001; SFU27075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7ET35; -.
DR STRING; 1224947.SAMN05216480_10159; -.
DR OrthoDB; 9805001at2; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000199138; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199138}.
FT ACT_SITE 196
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 255
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ SEQUENCE 331 AA; 36652 MW; 54E05E6227C4996E CRC64;
MHPLRRNRRL RTNESIRSLV RETSLSPQDF MFPMFVAEGK GVKTAIPSMP GMFRRSIDGT
VQEVKELWDL GIKAVNIYVK VSDNLKDNTG KEAWNKDGLM QQTIKAIKDA VPGMIVMPDV
ALDPYSIYGH DGIIENGQII NDATVDALTR MSISHAEAGA DFVAPSDMMD GRILAIREGL
ESNGFHNVGI MSYSAKYASA FYGPFRDALD SAPKDATVEV PKDKKTYQMD YANRIEAIKE
AIDDVEEGAD IVMVKPGMAY LDIVREVKDA VDVPVAVYQV SGEYAMVKAA AEKGWLDHDQ
IMMEQLMCIK RAGASIISTY FAKEAAIILN R
//
