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Database: UniProt
Entry: Q73IK2_WOLPM
LinkDB: Q73IK2_WOLPM
Original site: Q73IK2_WOLPM 
ID   Q73IK2_WOLPM            Unreviewed;       331 AA.
AC   Q73IK2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 116.
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:AAS13910.1};
GN   OrderedLocusNames=WD_0158 {ECO:0000313|EMBL:AAS13910.1};
OS   Wolbachia pipientis wMel.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=163164 {ECO:0000313|EMBL:AAS13910.1, ECO:0000313|Proteomes:UP000008215};
RN   [1] {ECO:0000313|EMBL:AAS13910.1, ECO:0000313|Proteomes:UP000008215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WMel {ECO:0000313|EMBL:AAS13910.1};
RX   PubMed=15024419; DOI=10.1371/journal.pbio.0020069;
RA   Wu M., Sun L.V., Vamathevan J., Riegler M., Deboy R., Brownlie J.C.,
RA   McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R.,
RA   Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F.,
RA   Nelson W.C., Mohamoud Y., Lee P., Berry K., Young M.B., Utterback T.,
RA   Weidman J., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H.,
RA   O'Neill S.L., Eisen J.A.;
RT   "Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a
RT   streamlined genome overrun by mobile genetic elements.";
RL   PLoS Biol. 2:327-341(2004).
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; AE017196; AAS13910.1; -; Genomic_DNA.
DR   RefSeq; WP_010962401.1; NZ_OX384529.1.
DR   AlphaFoldDB; Q73IK2; -.
DR   EnsemblBacteria; AAS13910; AAS13910; WD_0158.
DR   GeneID; 70035650; -.
DR   KEGG; wol:WD_0158; -.
DR   eggNOG; COG0113; Bacteria.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000008215; 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;  36601 MW;  2AFEF125C7FF0E86 CRC64;
     MFNFPNTRLR RRRSSKWVRN LTSENSLSVN DLVLPLFVHD REETTEPISG LPGVKCYSID
     GLVSIVKEAK DLGINAVAIF PVVDSKLKSE NAEEAYNSDN LICRAICAVK LKVPEIGIIA
     DVALDPYTIH GHDGILKDNQ MDVENDETIS VLCKQALALA KAGCDIVAPS DMMDGRVGRI
     RKSLDDNNFQ DVLILSYAVK YCSSFYAPFR QVVGSCGLSH SIDKSGYQMD YKNAHEAMCE
     IEMDINEGAD FIMIKPGMPY LDIIKTASDK FNFPIFAYQV SGEYAMIKAA ANNGWLDYDK
     VIYESLIGFK RAGASAIFTY AALDIAKNLS A
//
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