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Database: UniProt
Entry: E8PNS9_THESS
LinkDB: E8PNS9_THESS
Original site: E8PNS9_THESS 
ID   E8PNS9_THESS            Unreviewed;       326 AA.
AC   E8PNS9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 59.
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:ADW22734.1};
GN   OrderedLocusNames=TSC_c21310 {ECO:0000313|EMBL:ADW22734.1};
OS   Thermus scotoductus (strain ATCC 700910 / SA-01).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=743525 {ECO:0000313|EMBL:ADW22734.1, ECO:0000313|Proteomes:UP000008087};
RN   [1] {ECO:0000313|Proteomes:UP000008087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RA   Gounder K., Liesegang H., Brzuszkiewicz E., Wollherr A., Daniel R.,
RA   Gottschalk G., van Heerden E., Litthauer D.;
RT   "The genome sequence of Thermus scotoductus SA-01.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADW22734.1, ECO:0000313|Proteomes:UP000008087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RX   PubMed=22115438; DOI=10.1186/1471-2164-12-577;
RA   Gounder K., Brzuszkiewicz E., Liesegang H., Wollherr A., Daniel R.,
RA   Gottschalk G., Reva O., Kumwenda B., Srivastava M., Bricio C.,
RA   Berenguer J., van Heerden E., Litthauer D.;
RT   "Sequence of the hyperplastic genome of the naturally competent Thermus
RT   scotoductus SA-01.";
RL   BMC Genomics 12:577-577(2011).
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; CP001962; ADW22734.1; -; Genomic_DNA.
DR   RefSeq; WP_015717998.1; NC_014974.1.
DR   AlphaFoldDB; E8PNS9; -.
DR   STRING; 743525.TSC_c21310; -.
DR   KEGG; tsc:TSC_c21310; -.
DR   eggNOG; COG0113; Bacteria.
DR   HOGENOM; CLU_035731_0_1_0; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000008087; 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; cd00384; ALAD_PBGS; 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:PIRSR001415-3};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW   ECO:0000256|RuleBase:RU000515}; Zinc {ECO:0000256|PIRSR:PIRSR001415-3}.
FT   ACT_SITE        195
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   ACT_SITE        249
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   BINDING         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT   BINDING         126
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT   BINDING         205
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT   BINDING         217
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT   BINDING         234
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
FT   BINDING         275
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT   BINDING         314
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
SQ   SEQUENCE   326 AA;  35768 MW;  38F15C4A97324343 CRC64;
     MERPRRLRSP LLRPLVAEVE LSPRHLVLPV FVKEGGEPEE VSSMPGVFRH PLAQLPRLAE
     EVLKAGLGGM ILFGVLPEEE KDSLGHGAYA EEGIVQRAIR LLKREFPELL VMADTCLCEY
     TDHGHCGVVR EGPLGFYVDN DATLELLAKT ALSQAQAGAD VVAPSAMMDG QVKAIREALD
     QGGFAHVPIL SYAVKYASAF YGPFREAAGS APQFGDRTGY QMDPKAGLWD AMREASLDDL
     EGADMLMVKP ALPYLDVLYA LKGRFSKPLF AYQVSGEYAM LKAAGQRGWL DEKRAVLESL
     YALRRAGAQG ILTYYALEVA RWLKEA
//
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