ID A0A1W9KPX4_9BURK Unreviewed; 337 AA.
AC A0A1W9KPX4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-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=BWK72_18450 {ECO:0000313|EMBL:OQW86232.1};
OS Rhodoferax ferrireducens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=192843 {ECO:0000313|EMBL:OQW86232.1, ECO:0000313|Proteomes:UP000192505};
RN [1] {ECO:0000313|EMBL:OQW86232.1, ECO:0000313|Proteomes:UP000192505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A7 {ECO:0000313|EMBL:OQW86232.1};
RA Sharrar A.M., Flood B.E., Bailey J.V., Jones D.S., Biddanda B.,
RA Ruberg S.A., Marcus D.N., Dick G.J.;
RT "Novel large sulfur bacteria in the metagenomes of groundwater-fed
RT chemosynthetic microbial mats in the Lake Huron basin.";
RL Submitted (JAN-2017) 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:OQW86232.1}.
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DR EMBL; MTEI01000020; OQW86232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9KPX4; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000192505; 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 206
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 261
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ SEQUENCE 337 AA; 36858 MW; FCA020BAD321281F CRC64;
MTPYAPYPLG RPRRLRRDSF TRNLVRENLV TASDLIYPVF VVDGSQQRQP VLSMPGVERL
SLDLLLPVAE DCVKLGIPVM ALFPVIDQSL KTHDGREALN PDGLVPRVVQ ALKKEFPELG
IMCDVALDPF TSHGQDGLPD PAPGEDGYIM NDATVEILVK QALTQAGAGA DIVAPSDMMD
GRIGAIRQAL EANHFVHTRI MAYSAKYASA FYGPFRDAVG SSGNLGKSNK KVYQMDPGNS
DEALREVALD IAEGADMVMV KPGMPYLDIV RRVKDEFRVP TFAYQVSGEY AMLKAAAQNG
WLDHDAVMME SLLAFKRAGA DGVLTYFARD AARLINK
//
