(data stored in ACNUC29543 zone)

SWISSPROT: A5GQQ9_SYNR3

ID   A5GQQ9_SYNR3            Unreviewed;       333 AA.
AC   A5GQQ9;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 69.
DE   RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515};
DE            EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515};
GN   Name=hemB {ECO:0000313|EMBL:CAK27218.1};
GN   OrderedLocusNames=SynRCC307_0315 {ECO:0000313|EMBL:CAK27218.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27218.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|EMBL:CAK27218.1, ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RA   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen;
CC         Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24;
CC         Evidence={ECO:0000256|RuleBase:RU000515};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000256|RuleBase:RU000515}.
CC   -!- SIMILARITY: Belongs to the ALAD family.
CC       {ECO:0000256|RuleBase:RU004161}.
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DR   EMBL; CT978603; CAK27218.1; -; Genomic_DNA.
DR   RefSeq; WP_011934733.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0315; -.
DR   EnsemblBacteria; CAK27218; CAK27218; SynRCC307_0315.
DR   KEGG; syr:SynRCC307_0315; -.
DR   eggNOG; ENOG4105D52; Bacteria.
DR   eggNOG; COG0113; LUCA.
DR   HOGENOM; HOG000020323; -.
DR   KO; K01698; -.
DR   OMA; YQMDYAN; -.
DR   OrthoDB; 677575at2; -.
DR   BioCyc; SSP316278:G1GJL-312-MONOMER; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004655; F:porphobilinogen synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR001731; ALAD.
DR   InterPro; IPR030656; ALAD_AS.
DR   InterPro; IPR013785; Aldolase_TIM.
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;
DR   PRODOM; A5GQQ9.
DR   SWISS-2DPAGE; A5GQQ9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Lyase {ECO:0000256|RuleBase:RU000515, ECO:0000313|EMBL:CAK27218.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001415-5};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001415-5};
KW   Porphyrin biosynthesis {ECO:0000256|RuleBase:RU000515};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115}.
FT   ACT_SITE    196    196       Schiff-base intermediate with substrate.
FT                                {ECO:0000256|PIRSR:PIRSR001415-1}.
FT   ACT_SITE    256    256       Schiff-base intermediate with substrate.
FT                                {ECO:0000256|PIRSR:PIRSR001415-1}.
FT   METAL       241    241       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR001415-5}.
SQ   SEQUENCE   333 AA;  36327 MW;  CF72D252F0015456 CRC64;
     MDIAYRPRRL RRTPGLRAMV REHHVSAADF IYPLFVHEGA TNEPIGAMPG AQRWSLDGLL
     GEVGRAWDLG IRCVVLFPKV ADGLKTEDGS ECFNEGGLIP RAIRRIKQEH PGMTVMTDVA
     LDPYSCDGHD GIVSNEGIVL NDETVEILCR QAVTQAAAGA DLIGPSDMMD GRVGAIREAL
     DDEGYSHVGI ISYTAKYASA YYGPFREALD SAPRAAAGKP IPNDKSTYQM DPANSREALT
     EALLDEQEGA DIMMVKPGLA YLDIIHRLRA ETELPIAAYN VSGEYAMVKA AAEKGWIDER
     AVVLETLLSF KRAGADLILT YHACDAAEWL RHG
//

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