ID A0A0H2KRC9_9MICO Unreviewed; 344 AA.
AC A0A0H2KRC9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=FB00_05425 {ECO:0000313|EMBL:KLN35728.1};
OS Cellulosimicrobium funkei.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Cellulosimicrobium.
OX NCBI_TaxID=264251 {ECO:0000313|EMBL:KLN35728.1, ECO:0000313|Proteomes:UP000035265};
RN [1] {ECO:0000313|EMBL:KLN35728.1, ECO:0000313|Proteomes:UP000035265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U11 {ECO:0000313|EMBL:KLN35728.1,
RC ECO:0000313|Proteomes:UP000035265};
RA Hu C., Gong Y., Wan W., Jiang M.;
RT "Cellulosimicrobium funkei U11 genome.";
RL Submitted (MAY-2014) 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:KLN35728.1}.
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DR EMBL; JNBQ01000003; KLN35728.1; -; Genomic_DNA.
DR RefSeq; WP_047231823.1; NZ_JNBQ01000003.1.
DR AlphaFoldDB; A0A0H2KRC9; -.
DR STRING; 264251.FB00_05425; -.
DR PATRIC; fig|264251.5.peg.1113; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000035265; 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; cd00384; ALAD_PBGS; 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:UP000035265}.
FT ACT_SITE 209
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 219
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 230
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
FT BINDING 287
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 326
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
SQ SEQUENCE 344 AA; 36264 MW; 161F1D054F4854C9 CRC64;
MTHQLPVGHH RPRRLRTSPR VRRLVTETRV HASDLVLPLF VKEGLDAPRP ISSMPGVVQH
TEATLADAVR EAARAGVGGV MLFGIPAERD ATGTQADAAD GILQRGIRVA VEAAREHAGG
GPVVMADTCL DEFTDHGHCG VLAEGRDGGV VVDNDATLDR YASMAVAQAR AGADVVAPSG
MMDGQVGVIR EALDAAGFDD VGILAYSAKY ASAFYGPFRE AVDSALQGDR RTYQMDAGNA
REGLREADLD LAEGADMVMV KPAGSYLDVL AAVAEMSPVP VAAYQVSGEY AMIEAAAANG
WIDRRAAVTE SVLGIKRAGA DVILTYWATE LAGWLDENDG RTRA
//
