ID   HEM2_CHLTE              Reviewed;         328 AA.
AC   Q8KCJ0;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 40.
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=CT1431;
OS   Chlorobium tepidum.
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=1097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / TLS;
RX   MEDLINE=22103685; PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M.,
RA   Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F.,
RA   Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P.,
RA   Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B.,
RA   Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M.,
RA   Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a
RT   photosynthetic, anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
CC   -!- CATALYTIC ACTIVITY: 2 5-aminolevulinate = porphobilinogen + 2
CC       H(2)O.
CC   -!- ENZYME REGULATION: Stimulated by magnesium, inhibited by zinc.
CC   -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis;
CC       coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC   -!- SUBUNIT: Homooctamer (By similarity).
CC   -!- MISCELLANEOUS: Does not seem to have a metal requirement for
CC       activity.
CC   -!- SIMILARITY: Belongs to the ALADH family.
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DR   EMBL; AE006470; AAM72659.1; -; Genomic_DNA.
DR   RefSeq; NP_662317.1; -.
DR   HSSP; Q59643; 1B4K.
DR   SMR; Q8KCJ0; 10-328.
DR   GeneID; 1005979; -.
DR   GenomeReviews; AE006470_GR; CT1431.
DR   KEGG; cte:CT1431; -.
DR   NMPDR; fig|194439.1.peg.1411; -.
DR   TIGR; CT1431; -.
DR   HOGENOM; Q8KCJ0; -.
DR   OMA; Q8KCJ0; PELGVIT.
DR   BioCyc; CTEP194439:CT_1431-MON; -.
DR   BRENDA; 4.2.1.24; 189605.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004655; F:porphobilinogen synthase activity; IEA:EC.
DR   GO; GO:0006783; P:heme 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; Heme biosynthesis; Lyase; Magnesium;
KW   Porphyrin biosynthesis.
FT   CHAIN         1    328       Delta-aminolevulinic acid dehydratase.
FT                                /FTId=PRO_0000140497.
FT   ACT_SITE    253    253       By similarity.
SQ   SEQUENCE   328 AA;  36433 MW;  55556CA0D0632148 CRC64;
     MSQLDLLNIV HRPRRLRRTA ALRNLVQENT LTVNDLVFPL FVMPGTNAVE EVPSMPGSFR
     FTIDRAVEEC KELYDLGIQA IDLFGIPEKK TEDGSEAYND NGILQQAIRA IKKAVPELCI
     MTDVALDPFT PFGHDGLVRD GIILNDETVE VLQKMAVSHA EAGADFVSPS DMMDGRIGAI
     REALDESDHS DVGILSYAAK YASSFYGPFR DALHSAPQFG DKSTYQMNPA NTDEAMKEVE
     LDIIEGADIV MVKPGLAYLD IVWRTKERFD VPVAIYHVSG EYAMVKAAAA NGWIDEERVM
     MESLLCMKRA GADIIFTYYA KEAAKKLR
//