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Database: UniProt
Entry: E0WQE8_9ENTR
LinkDB: E0WQE8_9ENTR
Original site: E0WQE8_9ENTR 
ID   E0WQE8_9ENTR            Unreviewed;       375 AA.
AC   E0WQE8;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 50.
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:EFL92358.1};
GN   ORFNames=REG_0109 {ECO:0000313|EMBL:EFL92358.1};
OS   Candidatus Regiella insecticola LSR1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts; Candidatus Regiella.
OX   NCBI_TaxID=663321 {ECO:0000313|EMBL:EFL92358.1, ECO:0000313|Proteomes:UP000005726};
RN   [1] {ECO:0000313|EMBL:EFL92358.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LSR1 {ECO:0000313|EMBL:EFL92358.1};
RX   PubMed=19840097;
RA   Degnan P.H., Leonardo T.E., Cass B.N., Hurwitz B., Stern D., Gibbs R.A.,
RA   Richards S., Moran N.A.;
RT   "Dynamics of genome evolution in facultative symbionts of aphids.";
RL   Environ. Microbiol. 0:0-0(2009).
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; GL379589; EFL92358.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0WQE8; -.
DR   STRING; 663321.REG_0109; -.
DR   eggNOG; COG0113; Bacteria.
DR   HOGENOM; CLU_035731_0_0_6; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000005726; Miscellaneous, Scaffold Scaffold1.
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:UP000005726}.
FT   ACT_SITE        237
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   ACT_SITE        292
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   BINDING         277
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ   SEQUENCE   375 AA;  41728 MW;  162BCF447127304C CRC64;
     MPGARNLHVL MSSAPGALAA YHSLRFHLSE DNMSYLFTGT FPARRLRRLR RYDFSRRLTA
     ENQLTVNDLI YPLFIIEGEH RQEAIASMPG ISRMSIDLLL KEAEVVAKLG IPVIALFPVI
     DSSIKSINAE EAYNPNGLVQ RAVRALKKAV PELGVLTDVA LDPYTLHGHD GIVDKSSGYV
     INDTTNGILV RQALSHAEAG SDIIAPSDMM DGRIGAIRDA LENKKQANTQ IMAYSAKYAS
     CYYGPFRDAI GSRVKLKSID KKNYQMDPAN SHEALQEIAQ DLQEGADMVM IKPGMPYLDI
     VRRVKDTFYV PTFAYQVSGE YAMHMAAINN HWLPEKPAIM ESLLCFKRAG ADGVLTYFAK
     KVAQWLSEDQ FVVNQ
//
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