ID M9WTB6_9RICK Unreviewed; 331 AA.
AC M9WTB6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
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:AGJ99570.1};
GN ORFNames=wHa_00740 {ECO:0000313|EMBL:AGJ99570.1};
OS Wolbachia endosymbiont of Drosophila simulans wHa.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia.
OX NCBI_TaxID=1236909 {ECO:0000313|EMBL:AGJ99570.1, ECO:0000313|Proteomes:UP000013003};
RN [1] {ECO:0000313|EMBL:AGJ99570.1, ECO:0000313|Proteomes:UP000013003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=wHa {ECO:0000313|Proteomes:UP000013003};
RX PubMed=23593012;
RA Ellegaard K.M., Klasson L., Naslund K., Bourtzis K., Andersson S.G.;
RT "Comparative genomics of wolbachia and the bacterial species concept.";
RL PLoS Genet. 9:E1003381-E1003381(2013).
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; CP003884; AGJ99570.1; -; Genomic_DNA.
DR RefSeq; WP_015588802.1; NC_021089.1.
DR AlphaFoldDB; M9WTB6; -.
DR KEGG; wen:wHa_00740; -.
DR PATRIC; fig|1236909.3.peg.85; -.
DR HOGENOM; CLU_035731_0_0_5; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000013003; 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}.
FT ACT_SITE 200
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 331 AA; 36651 MW; D7E779585DEAF804 CRC64;
MFNFPNTRLR RRRSSKWVRN LTSENSLSVN DLVLPLFVHD REETTEPISG LPDVKCYSID
GLVSIVKEAK DLGINAVAIF PVVDSKLKSE NAEEAYNSDN LICRAICAVK LKVPEIGIIA
DIALDPYTIH GHDGILKDNQ MDVENDETVS ILCKQALALA ASGCDVVAPS DMMDGRIGRI
RKSLDDNNFQ DVLILSYAVK YCSSFYAPFR QVVGSCGLSH SIDKSGYQMD YKNAREAMCE
IEMDINEGAD FIMIKPGMPY LDIIKTASDK FNFPIFAYQV SGEYAMIKAA ANNGWLDYDK
VIYESLIGFK RAGASAIFTY AALDIAKNLS A
//
