HEM2_STAA8
ID HEM2_STAA8 Reviewed; 324 AA.
AC Q2FXR3; P50915;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=SAOUHSC_01772;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9358061; DOI=10.1016/s0378-1119(97)00372-7;
RA Kafala B., Sasarman A.;
RT "Isolation of the Staphylococcus aureus hemCDBL gene cluster coding for
RT early steps in heme biosynthesis.";
RL Gene 199:231-239(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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; U89396; AAC45835.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD30841.1; -; Genomic_DNA.
DR RefSeq; WP_000667126.1; NZ_LS483365.1.
DR RefSeq; YP_500277.1; NC_007795.1.
DR AlphaFoldDB; Q2FXR3; -.
DR SMR; Q2FXR3; -.
DR STRING; 1280.SAXN108_1695; -.
DR EnsemblBacteria; ABD30841; ABD30841; SAOUHSC_01772.
DR GeneID; 3919690; -.
DR KEGG; sao:SAOUHSC_01772; -.
DR PATRIC; fig|93061.5.peg.1616; -.
DR eggNOG; COG0113; Bacteria.
DR HOGENOM; CLU_035731_0_0_9; -.
DR OMA; YQMDYAN; -.
DR UniPathway; UPA00251; UER00318.
DR PRO; PR:Q2FXR3; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004655; F:porphobilinogen synthase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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 Reference proteome; Zinc.
FT CHAIN 1..323
FT /note="Delta-aminolevulinic acid dehydratase"
FT /id="PRO_0000247939"
FT ACT_SITE 195
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT ACT_SITE 248
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 314..315
FT /note="FA -> C (in Ref. 1; AAC45835)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="K -> N (in Ref. 1; AAC45835)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 36583 MW; BF24378E01E7C93E CRC64;
MKFDRHRRLR SSATMRDMVR ENHVRKEDLI YPIFVVEKDD VKKEIKSLPG VYQISLNLLE
SELKEAYDLG IRAIMFFGVP NSKDDIGTGA YIHDGVIQQA TRIAKKMYDD LLIVADTCLC
EYTDHGHCGV IDDHTHDVDN DKSLPLLVKT AISQVEAGAD IIAPSNMMDG FVAEIRRGLD
EAGYYNIPIM SYGVKYASSF FGPFRDAADS APSFGDRKTY QMDPANRLEA LRELESDLKE
GCDMMIVKPA LSYLDIVRDV KNHTNVPVVA YNVSGEYSMT KAAAQNGWID EERVVMEQMV
SMKRAGADMI ITYFAKDICR YLDK
