ID F2L4T7_THEU7 Unreviewed; 338 AA.
AC F2L4T7;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515};
DE EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515};
GN OrderedLocusNames=TUZN_1983 {ECO:0000313|EMBL:AEA13441.1};
OS Thermoproteus uzoniensis (strain 768-20).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=999630 {ECO:0000313|EMBL:AEA13441.1, ECO:0000313|Proteomes:UP000008138};
RN [1] {ECO:0000313|EMBL:AEA13441.1, ECO:0000313|Proteomes:UP000008138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=768-20 {ECO:0000313|EMBL:AEA13441.1,
RC ECO:0000313|Proteomes:UP000008138};
RX PubMed=21478349; DOI=10.1128/JB.00409-11;
RA Mardanov A.V., Gumerov V.M., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of the thermoacidophilic crenarchaeon
RT Thermoproteus uzoniensis 768-20.";
RL J. Bacteriol. 193:3156-3157(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=768-20;
RA Mardanov A.V., Gumerov V.M., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of the thermoacidophilic crenarchaeon
RT Thermoproteus uzoniensis 768-20.";
RL Submitted (MAR-2011) 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; CP002590; AEA13441.1; -; Genomic_DNA.
DR AlphaFoldDB; F2L4T7; -.
DR STRING; 999630.TUZN_1983; -.
DR KEGG; tuz:TUZN_1983; -.
DR eggNOG; arCOG04300; Archaea.
DR HOGENOM; CLU_035731_0_0_2; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000008138; 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}; Zinc {ECO:0000256|PIRSR:PIRSR001415-3}.
FT ACT_SITE 204
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 125
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 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
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 226
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
FT BINDING 284
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 323
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
SQ SEQUENCE 338 AA; 37431 MW; 9CAD7F117F45B319 CRC64;
MQLSFPTSRP RRLRANKLVR DAVAETSLSP DDFIMPIFVK DGAGKEPIDS MPGYFRWPVD
GSLVEHVEEA LSLGVNKFIL FGVLPDDVKD PEGKASYDPQ GVVPRAIRLL KETFGDRVLL
FADVCLCEYT DHGHCGVVVR DGRGWRIDND RTISIYAKEA VVYADAGADF VAPSGMMDGQ
VRAIRQALDA AGYQDVGIMA YSAKYASAFY GPFRVAASSA PKFGDRRTYQ MDPRNSREAV
KEVMLDIEEG ADIVMVKPAL AYLDVVRLVK DWFPWVPLAA YSVSGEYSMI KAAAKMGYLD
ERLVALEALF AIKRAGADLI LTYYALDAAR WLREGTPF
//
