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
//