ID A0A1X1QS36_9GAMM Unreviewed; 321 AA.
AC A0A1X1QS36;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=A6F72_08060 {ECO:0000313|EMBL:ORU94015.1};
OS Cycloclasticus sp. symbiont of Poecilosclerida sp. N.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Cycloclasticus.
OX NCBI_TaxID=1840472 {ECO:0000313|EMBL:ORU94015.1, ECO:0000313|Proteomes:UP000193416};
RN [1] {ECO:0000313|EMBL:ORU94015.1, ECO:0000313|Proteomes:UP000193416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Specimen N {ECO:0000313|EMBL:ORU94015.1};
RA Rubin Blum M., Dubilier N.;
RT "Short-chain alkanes fuel the metabolism of mussel and sponge
RT Cycloclasticus symbionts from deep-sea gas and oil seeps.";
RL Submitted (APR-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}.
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:ORU94015.1}.
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DR EMBL; LWTM01000062; ORU94015.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1QS36; -.
DR STRING; 1840472.A6F72_08060; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000193416; Unassembled WGS sequence.
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:UP000193416}.
FT ACT_SITE 188
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 243
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ SEQUENCE 321 AA; 34963 MW; A8ED8CEBBA56DDB5 CRC64;
MRNDDFSRRM MRETTLTVDD LICPVFVVDG ENQRQKITSM PGVERLSIDL LLQEAKEIFE
LGVPAIALFP VISEGSKTRL ADEAWNSDGL AQRAVRALKE ALPALGVITD VALDPFTTHG
QDGLVDESGY VLNDQTVDVL VKQALSHAQA GADVVAPSDM MDGRVGAIRE ALEAAGYTHT
RILAYSAKYA SSFYGPFRDA VRSAAQLGAG NKYSYQMDCA NTDEALVEVG LDIKEGADMV
MVKPGMLYLD IVRRVSEEFS VPVFAYQVSG EYAMLKAAAQ NGWLDEKATV LESLLAFKRA
GADGVLTYFA KDVASWLKES K
//
