ID V6AQ84_9ARCH Unreviewed; 327 AA.
AC V6AQ84;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515};
DE EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515};
GN Name=hemB {ECO:0000313|EMBL:CDI04826.1};
GN ORFNames=NITUZ_10021 {ECO:0000313|EMBL:CDI04826.1};
OS Candidatus Nitrosotenuis uzonensis.
OC Archaea; Nitrososphaerota; Nitrosotenuis.
OX NCBI_TaxID=1407055 {ECO:0000313|EMBL:CDI04826.1, ECO:0000313|Proteomes:UP000018159};
RN [1] {ECO:0000313|EMBL:CDI04826.1, ECO:0000313|Proteomes:UP000018159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N4 {ECO:0000313|EMBL:CDI04826.1,
RC ECO:0000313|Proteomes:UP000018159};
RX DOI=10.1371/journal.pone.0080835;
RA Lebedeva E.V., Hatzenpichler R., Pelletier E., Schuster N., Hauzmayer S.,
RA Bulaev A., Grigor'eva N.V., Galushko A., Schmid M., Palatinszky M.,
RA Le Paslier D., Daims H., Wagner M.;
RT "Enrichment and Genome Sequence of the Group I.1a Ammonia-Oxidizing
RT Archaeon ?Ca. Nitrosotenuis uzonensis? Representing a Clade Globally.";
RL PLoS ONE 0:0-0(2013).
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:CDI04826.1}.
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DR EMBL; CBTY010000001; CDI04826.1; -; Genomic_DNA.
DR RefSeq; WP_048193965.1; NZ_CBTY010000001.1.
DR AlphaFoldDB; V6AQ84; -.
DR STRING; 1407055.NITUZ_10021; -.
DR OrthoDB; 8493at2157; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000018159; 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: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 198
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 251
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
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 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT BINDING 208
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 220
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
FT BINDING 277
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 316
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
SQ SEQUENCE 327 AA; 36332 MW; 66A757D36201D41F CRC64;
MSAPFPTRRL RRLRKNEKMR NLVQEVTFSV NDLICPVFVQ ENLKSRTFVE SMPDIQRLPL
SDVTQEVQSI KDLGIPAIML FGIPEKKDEY GTGAFADDGI VQKAASEIRK SFGDSMVIMS
DVCLCQYTSS GHCGILNGNI IDNDSSLMTL SRIALSQAAS GVDIVSPSAM MDGQVKAIRN
ALDEKGFSDV GIMSHSAKHR SSFYNPFRDA ADCAPQFGDR KTYQVPFTNP REAMREIEMD
VSEGVDIVMV KPALSYLDLI AKTRERFNVP VSAYSVSGEY ALVKGAAKQG WINEDEIMAE
ILYSIKRAGA DMIVTYFAKK MAEYLNR
//
