ID A0A1H9P8P0_9RHOB Unreviewed; 330 AA.
AC A0A1H9P8P0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN04490244_10168 {ECO:0000313|EMBL:SER44457.1};
OS Tranquillimonas rosea.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tranquillimonas.
OX NCBI_TaxID=641238 {ECO:0000313|EMBL:SER44457.1, ECO:0000313|Proteomes:UP000198885};
RN [1] {ECO:0000313|EMBL:SER44457.1, ECO:0000313|Proteomes:UP000198885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23042 {ECO:0000313|EMBL:SER44457.1,
RC ECO:0000313|Proteomes:UP000198885};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOGU01000001; SER44457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9P8P0; -.
DR STRING; 641238.SAMN04490244_10168; -.
DR OrthoDB; 9805001at2; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000198885; Unassembled WGS sequence.
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; 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 Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW ECO:0000256|RuleBase:RU000515};
KW Reference proteome {ECO:0000313|Proteomes:UP000198885}.
FT ACT_SITE 200
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 254
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
SQ SEQUENCE 330 AA; 35626 MW; F98AAD1D7C9C71D9 CRC64;
MTQAPYPSTR FRRLRRTPAL RDLTRETSLS PGDLIWPVFV RDGEDAADPI PSMPGVHRLT
IDRLLPAVEE AATLGIPAVC LFPYTDPALK TELCEEAWNS DNLSNRAVRA IKDAVPEIAV
MTDVALDPYN INGHDGIVRD GVVVNDATVE ALVKMALAQA DSGADILGPS DMMDGRIGAM
RTALEDAGHT DVTIMSYSAK YASAFYGPFR DAVGASGALK GDKATYQMDP GNAAEALRLV
ERDLIEGADM VMVKPGMPYL DICRQVKDAF GVPTYAYQVS GEYAMIRGAA DQGWIDGEKV
MMESVLGFKR AGCDGILTYF APEVARRLAG
//