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 16-JUN-2009, entry version 24. DE RecName: Full=Delta-aminolevulinic acid dehydratase; DE Short=ALADH; DE Short=ALAD; DE EC=4.2.1.24; DE AltName: Full=Porphobilinogen synthase; GN Name=hemB; OrderedLocusNames=SAOUHSC_01772; OS Staphylococcus aureus (strain NCTC 8325). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=93061; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=98019093; 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 RT for early steps in heme biosynthesis."; RL Gene 199:231-239(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., RA Iandolo J.J.; RT "The Staphylococcus aureus NCTC8325 genome."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2 5-aminolevulinate = porphobilinogen + 2 CC H(2)O. CC -!- COFACTOR: Zinc (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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U89396; AAC45835.1; -; Genomic_DNA. DR EMBL; CP000253; ABD30841.1; -; Genomic_DNA. DR RefSeq; YP_500277.1; -. DR GeneID; 3919690; -. DR GenomeReviews; CP000253_GR; SAOUHSC_01772. DR KEGG; sao:SAOUHSC_01772; -. DR HOGENOM; Q2FXR3; -. DR OMA; Q2FXR3; AESTPQF. DR BioCyc; SAUR93061:SAOUHSC_01772-MON; -. DR GO; GO:0004655; F:porphobilinogen synthase activity; IEA:EC. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006779; P:porphyrin biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR001731; 4pyrrol_synth_porphobiln_synth. DR InterPro; IPR013785; Aldolase_TIM. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR PANTHER; PTHR11458; AlaD_dehydratase; 1. DR Pfam; PF00490; ALAD; 1. DR PIRSF; PIRSF001415; Porphbilin_synth; 1. DR PRINTS; PR00144; DALDHYDRTASE. DR ProDom; PD002304; AlaD_dehydratase; 1. DR PROSITE; PS00169; D_ALA_DEHYDRATASE; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Porphyrin biosynthesis; Zinc. FT CHAIN 1 323 Delta-aminolevulinic acid dehydratase. FT /FTId=PRO_0000247939. FT REGION 115 133 Zinc-binding (By similarity). FT ACT_SITE 248 248 By similarity. FT CONFLICT 314 315 FA -> C (in Ref. 1; AAC45835). FT CONFLICT 324 324 K -> N (in Ref. 1; AAC45835). 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 //