ID A0A0S6WZV1_9SPHN Unreviewed; 329 AA.
AC A0A0S6WZV1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 03-MAY-2023, entry version 22.
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=MBENS4_1616 {ECO:0000313|EMBL:GAM04618.1};
OS Novosphingobium sp. MBES04.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1206458 {ECO:0000313|EMBL:GAM04618.1};
RN [1] {ECO:0000313|EMBL:GAM04618.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBES04 {ECO:0000313|EMBL:GAM04618.1};
RA Ohta Y., Nishi S., Kobayashi K., Tsubouchi T., Iida K., Tanizaki A.,
RA Kurosawa K., Adachi A., Nishihara M., Sato R., Hasegawa R., Hatada Y.;
RT "Draft Genome Sequence of Novosphingobium sp. Strain MBES04, Isolated from
RT Sunken Wood from Suruga Bay, Japan.";
RL Genome Announc. 3:e01373-14(2015).
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; DF850488; GAM04618.1; -; Genomic_DNA.
DR RefSeq; WP_039389951.1; NZ_DF850488.1.
DR AlphaFoldDB; A0A0S6WZV1; -.
DR STRING; 1206458.MBENS4_1616; -.
DR HOGENOM; CLU_035731_0_0_5; -.
DR OrthoDB; 9805001at2; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000053513; 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 199
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 253
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ SEQUENCE 329 AA; 35621 MW; C73E08EAADDA62FF CRC64;
MTYPHTRLRR ARATAWSRAL HRETILTPAD LIWPVFVTDG EGVEEPIASL PGVSRWSVDL
LVERAKEAVE LGIPCLALFP NTQPERRSAK GEEALNPDNL MCRAIRAIRE ACGDSIGLLT
DVALDPYTDH GQDGLIDAEG YVLNDDTVEA LVGQALNQAR AGADIIAPSD MMDGRIEAIR
AALEAEGHIN VQIMSYAAKY ASAFYGPFRD AVGSRGLLKG DKKTYQMDPA NTEEALREVE
LDLAEGADSV MVKPGLPYLD IVRRVKEAFE VPVFAYQVSG EYAMIEAAVA AGAGDRDALV
LETLLAFKRA GCSGILTYHA VHAARLLNG
//
