ID A0A1J4YVG6_9PROT Unreviewed; 333 AA.
AC A0A1J4YVG6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=AUJ86_05965 {ECO:0000313|EMBL:OIO78210.1};
OS Hydrogenophilaceae bacterium CG1_02_62_390.
OC Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales;
OC Hydrogenophilaceae.
OX NCBI_TaxID=1805218 {ECO:0000313|EMBL:OIO78210.1, ECO:0000313|Proteomes:UP000182441};
RN [1] {ECO:0000313|EMBL:OIO78210.1, ECO:0000313|Proteomes:UP000182441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_62_390 {ECO:0000313|EMBL:OIO78210.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIO78210.1}.
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DR EMBL; MNXE01000036; OIO78210.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4YVG6; -.
DR STRING; 1805218.AUJ86_05965; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000182441; 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}.
FT ACT_SITE 202
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 257
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ SEQUENCE 333 AA; 36358 MW; 55F108E084201A99 CRC64;
MFDLSSFPHK RMRRMRHDPF SRNLMRETVL TSADLILPVF VLDGEGREEA VASMPGVKRL
SLDKLYLVAE ECLQLGIPAL ALFPVIDAPL KSETAEEAYN PNGLVPRTVA ALKARFPALG
IITDVALDPY TSHGQDGLID AAGYVLNDET IAVLTRQAEC HARAGADVVA PSDMMDGRIH
AVREALDSAG FIHTRILAYS AKYASSFYGP FRDAVGSSAN LGAGDKYTYQ MDPANTDEAL
WEVGLDLQEG ADMVMVKPGM PYLDVVRNIK QTFKAPTCVY QVSGEYAMLK AAAQNGWLNE
RACVLESLLS FKRAGADAVL TYYALDAARW LQA
//
