ID   HEM2_PHYPA              Reviewed;         430 AA.
AC   Q43058;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=Delta-aminolevulinic acid dehydratase, chloroplastic;
DE            Short=ALADH;
DE            EC=4.2.1.24;
DE   AltName: Full=Porphobilinogen synthase;
DE   Flags: Precursor;
GN   Name=HEMB; Synonyms=ALAD;
OS   Physcomitrella patens (Moss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Moss Superclass V; Bryopsida; Funariidae; Funariales; Funariaceae;
OC   Physcomitrella.
OX   NCBI_TaxID=3218;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Gwarek M.A.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 2 5-aminolevulinate = porphobilinogen + 2
CC       H(2)O.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis;
CC       coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC   -!- SUBUNIT: Homooctamer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the ALADH family.
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DR   EMBL; X89886; CAA61978.1; -; mRNA.
DR   PIR; S58169; S58169.
DR   HSSP; Q59643; 1GZG.
DR   BRENDA; 4.2.1.24; 3698.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004655; F:porphobilinogen synthase activity; IEA:EC.
DR   GO; GO:0015995; P:chlorophyll 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   PRINTS; PR00144; DALDHYDRTASE.
DR   ProDom; PD002304; AlaD_dehydratase; 1.
DR   PROSITE; PS00169; D_ALA_DEHYDRATASE; 1.
PE   2: Evidence at transcript level;
KW   Chlorophyll biosynthesis; Chloroplast; Lyase; Magnesium; Plastid;
KW   Porphyrin biosynthesis; Transit peptide.
FT   TRANSIT       1      ?       Chloroplast (Potential).
FT   CHAIN         ?    430       Delta-aminolevulinic acid dehydratase,
FT                                chloroplastic.
FT                                /FTId=PRO_0000013318.
FT   REGION      220    238       Magnesium-binding (By similarity).
FT   ACT_SITE    352    352       By similarity.
SQ   SEQUENCE   430 AA;  46140 MW;  FD1A477A28DEA399 CRC64;
     MVGVMMAAAA TPGCRVSQAL TACSSHEGLR RVAPVFGPGV VSVSAPCKLP RKLNVQAVAE
     PIAKSSPRTI EECEANVVAG NAPAAPPVPA KPSAPEGTPA ISPLVMPARP RRNRRSPALR
     AAFQETTISP ANFILPLFVH EGEQNAPIGA MPGCQRLGWR HGLIDEVYKA RDVGVNSVVL
     FPKVPDALKS STGDEAYNPD GLVPRCIRLL KAIPDLVIYT DVALDPYSSD GHDGIVREDG
     LIMNDETVHQ LCKQAVAQAQ AGADVVSPSD MMDGRVGAIR KALDLAGHQD VSIIAYTAKY
     ASAFYGPSRE ALDSNPRFGD KKTYQMNPAN YREALIETRM DEAEGADILM VKPAMPYLDV
     IRLLRDNTAL PISAYQVSGE YSMIRAGCRG MLDEKKAVLE SLLSIRRAGA DVILTYFAIQ
     AAQWLCAERV
//