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Database: UniProt
Entry: A0A191HWT7_9FIRM
LinkDB: A0A191HWT7_9FIRM
Original site: A0A191HWT7_9FIRM 
ID   A0A191HWT7_9FIRM        Unreviewed;        90 AA.
AC   A0A191HWT7;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|ARBA:ARBA00020771};
DE            EC=4.2.1.24 {ECO:0000256|ARBA:ARBA00012053};
DE   AltName: Full=Porphobilinogen synthase {ECO:0000256|ARBA:ARBA00032837};
GN   ORFNames=AZF37_06985 {ECO:0000313|EMBL:AMP20936.1};
OS   endosymbiont 'TC1' of Trimyema compressum.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=243899 {ECO:0000313|EMBL:AMP20936.1, ECO:0000313|Proteomes:UP000196836};
RN   [1] {ECO:0000313|EMBL:AMP20936.1, ECO:0000313|Proteomes:UP000196836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC1 {ECO:0000313|EMBL:AMP20936.1};
RA   Shinzato N., Aoyama H., Saitoh S., Nikoh N., Nakano K., Shimoji M.,
RA   Shinzato M., Satou K., Teruya K., Hirano T., Yamada T., Nobu M.K.,
RA   Tamaki H., Sanghwa P., Kamagata Y.;
RT   "Complete genome sequence of the intracellular bacterial symbiont 'TC1' in
RT   the anaerobic ciliate Trimyema compressum.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles.
CC       Binds two molecules of 5-aminolevulinate per subunit, each at a
CC       distinct site, and catalyzes their condensation to form
CC       porphobilinogen. {ECO:0000256|ARBA:ARBA00025628}.
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   -!- 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|ARBA:ARBA00011823}.
CC   -!- SIMILARITY: Belongs to the ALAD family.
CC       {ECO:0000256|ARBA:ARBA00008055}.
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DR   EMBL; CP014606; AMP20936.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A191HWT7; -.
DR   KEGG; ett:AZF37_06985; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000196836; Chromosome.
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   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR001731; ALAD.
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   SMART; SM01004; ALAD; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196836}.
SQ   SEQUENCE   90 AA;  10085 MW;  E26383D3B288C734 CRC64;
     MENQFYYSYD TVGKIIDESL KVGVSSFMLF GIPLKKDSIG TEAYKEDGII QNTLRTIKGF
     YGDSVNLISD VCLCEYTDHG HCGIIQKSKC
//
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