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Database: UniProt
Entry: F5Y4R7_RAMTT
LinkDB: F5Y4R7_RAMTT
Original site: F5Y4R7_RAMTT 
ID   F5Y4R7_RAMTT            Unreviewed;       336 AA.
AC   F5Y4R7;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|ARBA:ARBA00020771, ECO:0000256|RuleBase:RU000515};
DE            EC=4.2.1.24 {ECO:0000256|ARBA:ARBA00012053, ECO:0000256|RuleBase:RU000515};
GN   Name=hemB {ECO:0000313|EMBL:AEG91385.1};
GN   OrderedLocusNames=Rta_03150 {ECO:0000313|EMBL:AEG91385.1};
OS   Ramlibacter tataouinensis (strain ATCC BAA-407 / DSM 14655 / LMG 21543 /
OS   TTB310).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ramlibacter.
OX   NCBI_TaxID=365046 {ECO:0000313|EMBL:AEG91385.1, ECO:0000313|Proteomes:UP000008385};
RN   [1] {ECO:0000313|Proteomes:UP000008385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC   {ECO:0000313|Proteomes:UP000008385};
RA   Barakat M., Ortet P., De Luca G., Jourlin-Castelli C., Ansaldi M., Py B.,
RA   Fichant G., Coutinho P., Voulhoux R., Bastien O., Roy S., Marechal E.,
RA   Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V., DuBow M.,
RA   Barras F., Heulin T.;
RT   "Genome of the cyst-dividing bacterium Ramlibacter tataouinensis.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEG91385.1, ECO:0000313|Proteomes:UP000008385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC   {ECO:0000313|Proteomes:UP000008385};
RX   PubMed=21912644; DOI=10.1371/journal.pone.0023784;
RA   De Luca G., Barakat M., Ortet P., Fochesato S., Jourlin-Castelli C.,
RA   Ansaldi M., Py B., Fichant G., Coutinho P.M., Voulhoux R., Bastien O.,
RA   Marechal E., Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V.,
RA   Dubow M.S., Barras F., Barbe V., Weissenbach J., Mihalcescu I.,
RA   Vermeglio A., Achouak W., Heulin T.;
RT   "The Cyst-Dividing Bacterium Ramlibacter tataouinensis TTB310 Genome
RT   Reveals a Well-Stocked Toolbox for Adaptation to a Desert Environment.";
RL   PLoS ONE 6:E23784-E23784(2011).
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|ARBA:ARBA00001227,
CC         ECO:0000256|RuleBase:RU000515};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004694}.
CC   -!- SUBUNIT: Homooctamer. {ECO:0000256|RuleBase:RU000515}.
CC   -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000256|ARBA:ARBA00008055,
CC       ECO:0000256|RuleBase:RU004161}.
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DR   EMBL; CP000245; AEG91385.1; -; Genomic_DNA.
DR   RefSeq; WP_013899618.1; NC_015677.1.
DR   AlphaFoldDB; F5Y4R7; -.
DR   STRING; 365046.Rta_03150; -.
DR   KEGG; rta:Rta_03150; -.
DR   PATRIC; fig|365046.3.peg.323; -.
DR   eggNOG; COG0113; Bacteria.
DR   HOGENOM; CLU_035731_0_0_4; -.
DR   OMA; YQMDYAN; -.
DR   OrthoDB; 9805001at2; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000008385; 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:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04823; ALAD_PBGS_aspartate_rich; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR001731; ALAD.
DR   InterPro; IPR030656; ALAD_AS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   PANTHER; PTHR11458; DELTA-AMINOLEVULINIC ACID DEHYDRATASE; 1.
DR   PANTHER; PTHR11458:SF0; DELTA-AMINOLEVULINIC ACID DEHYDRATASE; 1.
DR   Pfam; PF00490; ALAD; 1.
DR   PIRSF; PIRSF001415; Porphbilin_synth; 1.
DR   PRINTS; PR00144; DALDHYDRTASE.
DR   SMART; SM01004; ALAD; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00169; D_ALA_DEHYDRATASE; 1.
PE   3: Inferred from homology;
KW   Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000515};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001415-5};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001415-5};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW   ECO:0000256|RuleBase:RU000515};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008385}.
FT   ACT_SITE        202
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   ACT_SITE        257
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   BINDING         242
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ   SEQUENCE   336 AA;  36724 MW;  944B3B9D4E8A601F CRC64;
     MTLHAPYPHG RPRRLRRDDF TRNLVREHTL TPHDLIYPVF VLDGRGRREA VASMPGVERL
     SLDLLLPVAE DCVALGIPVM ALFPVIDASL KTEDGREAWN AEGLVPRVVR ELKQRFPQLG
     VMTDVALDPF TSHGQDGLLD ATGYILNDET VQVLTRQALV QAEAGVDIVA PSDMMDGRIG
     AIRAALESRG AIHTRIMAYS AKYASAFYGP FRDAVGSAAN LGKGNKKVYQ MDPGNTDEAL
     REVALDIAEG ADMVMVKPGM PYLDVVRRVK DEFRVPTFAY QVSGEYAMLK AAAGNGWLDH
     DAVMMESLLA FKRAGADGVL TYFALDAARA LLGGRQ
//
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