ID HEM2_STAAW Reviewed; 324 AA.
AC P64335; Q99TJ3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 01-MAY-2013, entry version 55.
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=MW1612;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A.,
RA Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L.,
RA Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-
RT acquired MRSA.";
RL Lancet 359:1819-1827(2002).
CC -!- FUNCTION: Catalyzes an early step in the biosynthesis of
CC tetrapyrroles. Binds two molecules of 5-aminolevulinate per
CC subunit, each at a distinct site, and catalyzes their condensation
CC to form porphobilinogen (By similarity).
CC -!- CATALYTIC ACTIVITY: 2 5-aminolevulinate = porphobilinogen + 2
CC H(2)O.
CC -!- COFACTOR: Binds 1 zinc ion per monomer (By similarity).
CC -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis;
CC coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC -!- SUBUNIT: Homooctamer (By similarity).
CC -!- SIMILARITY: Belongs to the ALADH family.
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DR EMBL; BA000033; BAB95477.1; -; Genomic_DNA.
DR RefSeq; NP_646429.1; NC_003923.1.
DR ProteinModelPortal; P64335; -.
DR SMR; P64335; 5-318.
DR STRING; 196620.MW1612; -.
DR EnsemblBacteria; BAB95477; BAB95477; BAB95477.
DR GeneID; 1003724; -.
DR KEGG; sam:MW1612; -.
DR PATRIC; 19569838; VBIStaAur44266_1680.
DR eggNOG; COG0113; -.
DR HOGENOM; HOG000020323; -.
DR KO; K01698; -.
DR OMA; MIISYHA; -.
DR ProtClustDB; PRK09283; -.
DR BioCyc; SAUR196620:GJ9Z-1635-MONOMER; -.
DR UniPathway; UPA00251; UER00318.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004655; F:porphobilinogen synthase activity; IEA:EC.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001731; Porphobilinogen_synth.
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 Complete proteome; Heme biosynthesis; Lyase; Magnesium; Metal-binding;
KW Porphyrin biosynthesis; Zinc.
FT CHAIN 1 324 Delta-aminolevulinic acid dehydratase.
FT /FTId=PRO_0000140515.
FT ACT_SITE 195 195 Schiff-base intermediate with substrate
FT (By similarity).
FT ACT_SITE 248 248 Schiff-base intermediate with substrate
FT (By similarity).
FT METAL 118 118 Zinc; catalytic (By similarity).
FT METAL 120 120 Zinc; catalytic (By similarity).
FT METAL 128 128 Zinc; catalytic (By similarity).
FT METAL 233 233 Magnesium (By similarity).
FT BINDING 205 205 Substrate 1 (By similarity).
FT BINDING 217 217 Substrate 1 (By similarity).
FT BINDING 274 274 Substrate 2 (By similarity).
FT BINDING 313 313 Substrate 2 (By similarity).
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
//
