(data stored in ACNUC7421 zone)

HOGENOM: CHLTB_1_PE1

ID   CHLTB_1_PE1                          STANDARD;      PRT;   338 AA.
AC   CHLTB_1_PE1; B0BA87;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Delta-aminolevulinic acid dehydratase; EC=4.2.1 24;
DE   (CHLTB_1.PE1).
GN   Name=hemB; OrderedLocusNames=CTLon_0001;
OS   CHLAMYDIA TRACHOMATIS L2B/UCH-1/PROCTITIS.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=471473;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CHLTB_1.PE1.
CC       Chlamydia trachomatis L2b/UCH-1/proctitis, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:B0BA87_CHLTB
CC   -!- CATALYTIC ACTIVITY: 2 5-aminolevulinate = porphobilinogen + 2
CC       H(2)O.
CC   -!- SUBUNIT: Homooctamer (By similarity).
CC   -!- SIMILARITY: Belongs to the ALADH family.
CC   -!- GENE_FAMILY: HOG000020323 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B0BA87; -.
DR   EMBL; AM884177; CAP06399.1; -; Genomic_DNA.
DR   RefSeq; YP_001653104.1; NC_010280.1.
DR   ProteinModelPortal; B0BA87; -.
DR   STRING; B0BA87; -.
DR   GeneID; 5859500; -.
DR   GenomeReviews; AM884177_GR; CTLon_0001.
DR   KEGG; ctl:CTLon_0001; -.
DR   OMA; FTSHGHD; -.
DR   ProtClustDB; PRK09283; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004655; F:porphobilinogen synthase activity; IEA:EC.
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   PROSITE; PS00169; D_ALA_DEHYDRATASE; 1.
DR   HOGENOMDNA; CHLTB_1.PE1; -.
KW   delta-aminolevulinic acid dehydratase;
KW   Complete proteome; Lyase; Magnesium; Metal-binding;
KW   Porphyrin biosynthesis.
SQ   SEQUENCE   338 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTRLPLLKRP RRNRKSAAVR SIIQETQLCS SDLIWPIFLK DGSGIREEIE SMPGVYRWSL
     DMVSKELERL CTIGLKAVIL FPVIDANKKE QFGSYASHPY NIVCKGIQAI KKSFPELCVI
     SDIALDPFTT SGHDGIFHNN YVINDESVRV YGGIAVMHAE MGADIVAPSD MMDGRVKHIR
     EQMDQMGFVN TGILSYSAKY ASALYGPFRD ALSSHLQSGD KRTYQMDPAN VQEALLECQL
     DEEEGADMVM IKPAGFYLDV IVKARENTHL PVVAYQVSGE FSMIMAACLH GWLNKESVIK
     ESLLAIKRAG ATAIISYATP WVLEWLAKDA LPFERSVL
//

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