HEM2_SYNE7
ID HEM2_SYNE7 Reviewed; 326 AA.
AC P43087; Q31M97;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Delta-aminolevulinic acid dehydratase;
DE Short=ALAD;
DE Short=ALADH;
DE EC=4.2.1.24;
DE AltName: Full=Porphobilinogen synthase;
GN Name=hemB; OrderedLocusNames=Synpcc7942_1792;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8123787; DOI=10.1007/bf00024112;
RA Jones M.C., Jenkins J.M., Smith A.G., Howe C.J.;
RT "Cloning and characterisation of genes for tetrapyrrole biosynthesis from
RT the cyanobacterium Anacystis nidulans R2.";
RL Plant Mol. Biol. 24:435-448(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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 porphobilinogen
CC (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per monomer. {ECO:0000250};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC -!- SUBUNIT: Homooctamer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000305}.
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DR EMBL; X70434; CAA49892.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57822.1; -; Genomic_DNA.
DR RefSeq; WP_011244611.1; NC_007604.1.
DR AlphaFoldDB; P43087; -.
DR SMR; P43087; -.
DR STRING; 1140.Synpcc7942_1792; -.
DR PRIDE; P43087; -.
DR EnsemblBacteria; ABB57822; ABB57822; Synpcc7942_1792.
DR KEGG; syf:Synpcc7942_1792; -.
DR eggNOG; COG0113; Bacteria.
DR HOGENOM; CLU_035731_0_0_3; -.
DR OMA; YMDIIWR; -.
DR OrthoDB; 677575at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1792-MON; -.
DR UniPathway; UPA00251; UER00318.
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 Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR001731; ALAD.
DR InterPro; IPR030656; ALAD_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR PANTHER; PTHR11458; PTHR11458; 1.
DR Pfam; PF00490; ALAD; 1.
DR PIRSF; PIRSF001415; Porphbilin_synth; 1.
DR PRINTS; PR00144; DALDHYDRTASE.
DR SMART; SM01004; ALAD; 1.
DR PROSITE; PS00169; D_ALA_DEHYDRATASE; 1.
PE 3: Inferred from homology;
KW Heme biosynthesis; Lyase; Magnesium; Metal-binding; Porphyrin biosynthesis;
KW Zinc.
FT CHAIN 1..326
FT /note="Delta-aminolevulinic acid dehydratase"
FT /id="PRO_0000140520"
FT ACT_SITE 198
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT ACT_SITE 251
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 287
FT /note="A -> R (in Ref. 1; CAA49892)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 35574 MW; 0C4F44658CEB37BF CRC64;
MFPTHRPRRL RSSETLRRMV RETTLTSADF IYPLFAVPGE GVAKEVTSMP GVYQLSIDKI
VEEAKEVYDL GIPSIILFGI PTDKDNDATG AWHDCGIVQK AATAVKEAVP ELIVAADTCL
CEYTPHGHCG YLEVGDLSGR VLNDPTLELL RKTAVSQAKA GADIIAPSGM MDGFVATIRD
ALDEAGFSDT PIMAYSAKYA SAYYGPFRDA AESTPQFGDR RTYQMDPGNS REALKEVELD
VAEGADIVMV KPALSYMDII CRIKETTDLP VAAYNVSGEY SMVKAAALNG WIDEERVVLE
TLTSFKRAGA DLILTYHAKD AARWLA
