ID Q1RI13_RICBR Unreviewed; 330 AA.
AC Q1RI13;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 94.
DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|ARBA:ARBA00020771};
DE EC=4.2.1.24 {ECO:0000256|ARBA:ARBA00012053};
DE AltName: Full=Porphobilinogen synthase {ECO:0000256|ARBA:ARBA00032837};
GN Name=hemB {ECO:0000313|EMBL:ABE05001.1};
GN OrderedLocusNames=RBE_0920 {ECO:0000313|EMBL:ABE05001.1};
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407 {ECO:0000313|EMBL:ABE05001.1, ECO:0000313|Proteomes:UP000001951};
RN [1] {ECO:0000313|EMBL:ABE05001.1, ECO:0000313|Proteomes:UP000001951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C {ECO:0000313|EMBL:ABE05001.1,
RC ECO:0000313|Proteomes:UP000001951};
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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 -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004694}.
CC -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000256|ARBA:ARBA00008055,
CC ECO:0000256|RuleBase:RU004161}.
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DR EMBL; CP000087; ABE05001.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1RI13; -.
DR KEGG; rbe:RBE_0920; -.
DR eggNOG; COG0113; Bacteria.
DR HOGENOM; CLU_035731_0_0_5; -.
DR OMA; YQMDYAN; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000001951; 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; 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.
PE 3: Inferred from homology;
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ABE05001.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001415-5};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001415-5};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000001951}.
FT ACT_SITE 201
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 255
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ SEQUENCE 330 AA; 36910 MW; 4EC9CFC3353A8C9F CRC64;
MMRYIMYPLI RLRRNRKAAW LRDLVAETTL RVEDLVLPLF VVEGHNQRQE IKTLPDIYRL
SIDQVIETAR KAADLGIKAI ALFPCIDQSL KNENGDEAYN LDNLMCRTIR SIKNAGINIG
IICDVALDPY TTHGHDGIIH NGEVDNDKSV KALCNQALTL AKAGVDIVAP SDMMDGRIMA
IREYLDKEHF INVGILAYAA KYASSFYGLY RDAVGSTKKT YLDKASYQLD IRNIKEAMLE
IEHDIAEGAD MVMVKPGMMF LDVIREAANN FNTKIFAYQI TAEYAMLKFA ANAGAIDFEK
GLLESLISFK RAGASGIFTY AALEAAELYL
//