ID J1S541_9ACTN Unreviewed; 505 AA.
AC J1S541;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
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 ORFNames=SU9_16052 {ECO:0000313|EMBL:EJJ05942.1};
OS Streptomyces auratus AGR0001.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ05942.1};
RN [1] {ECO:0000313|EMBL:EJJ05942.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ05942.1};
RX PubMed=22965094; DOI=10.1128/JB.01155-12;
RA Han X., Li M., Ding Z., Zhao J., Ji K., Wen M., Lu T.;
RT "Genome Sequence of Streptomyces auratus Strain AGR0001, a Phoslactomycin-
RT Producing Actinomycete.";
RL J. Bacteriol. 194:5472-5473(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJJ05942.1}.
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DR EMBL; AJGV01000096; EJJ05942.1; -; Genomic_DNA.
DR AlphaFoldDB; J1S541; -.
DR STRING; 1160718.SU9_16052; -.
DR PATRIC; fig|1160718.3.peg.3246; -.
DR eggNOG; COG0113; Bacteria.
DR HOGENOM; CLU_539593_0_0_11; -.
DR UniPathway; UPA00251; UER00318.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; cd00384; ALAD_PBGS; 1.
DR CDD; cd16936; HATPase_RsbW-like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR001731; ALAD.
DR InterPro; IPR030656; ALAD_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036890; HATPase_C_sf.
DR PANTHER; PTHR11458; DELTA-AMINOLEVULINIC ACID DEHYDRATASE; 1.
DR PANTHER; PTHR11458:SF0; DELTA-AMINOLEVULINIC ACID DEHYDRATASE; 1.
DR Pfam; PF00490; ALAD; 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 Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW ECO:0000256|RuleBase:RU000515}.
FT REGION 150..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 505 AA; 53973 MW; AA2215A9912EFB1B CRC64;
MNQRITRTSS SVTGPAPALR FSVPLSATRR GARLARLLAT EQLRSWGLPF DPSLLLVAEL
AANAVLHGRV AGRCFRLGLV VTSPATLRIE VTDTRGDRLP VRAPDAGGLL AESGRGLLLV
AELADRWGIE EGPVPCKTVW ASSISARPLR TGGLSDPSAP TTRRQRQGQS GRSVGGMTKY
GSFPGARPRR LRTTPAMRRM VAEHRLHPSD LILPAFVREG ISEPVPISAM PGVVQHTRDT
LRKAAVEAVE AGVAGIMLFG VPEDAKKDAV GTAGTDPDGI LQVAIRDVRA EVGDDLVIMS
DLCLDEYTDH GHCGVLDADG RVDNDATLER YAEMAQVQAD AGVHAVGPSG MMDGQVGVVR
DALDQTGHED VSILAYTAKY SSAFYGPFRE AVGSSLKGDR KTYQQDPANL RESLRELALD
LDEGADMVMV KPALPYLDVL AKIADSVDVP VAAYQISGEY AMIEAAAEKG WIDRDKAILE
ALTGIKRAGA NMILTYWATE VARGL
//
