ID A0A077LYN5_9MICO Unreviewed; 280 AA.
AC A0A077LYN5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|ARBA:ARBA00020771};
DE EC=4.2.1.24 {ECO:0000256|ARBA:ARBA00012053};
DE AltName: Full=Porphobilinogen synthase {ECO:0000256|ARBA:ARBA00032837};
GN Name=hemB {ECO:0000313|EMBL:CCH78736.1};
GN ORFNames=BN12_3320001 {ECO:0000313|EMBL:CCH78736.1};
OS Tetrasphaera japonica T1-X7.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1194083 {ECO:0000313|EMBL:CCH78736.1, ECO:0000313|Proteomes:UP000035721};
RN [1] {ECO:0000313|EMBL:CCH78736.1, ECO:0000313|Proteomes:UP000035721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T1-X7 {ECO:0000313|EMBL:CCH78736.1,
RC ECO:0000313|Proteomes:UP000035721};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
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 -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004694}.
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:CCH78736.1}.
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DR EMBL; CAJB01000260; CCH78736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077LYN5; -.
DR STRING; 1194083.BN12_3320001; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000035721; 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 Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR001731; ALAD.
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.
PE 3: Inferred from homology;
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:CCH78736.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001415-5};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001415-5};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000035721}.
FT ACT_SITE 153
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 205
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT BINDING 163
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 174
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
FT BINDING 231
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 270
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
SQ SEQUENCE 280 AA; 29288 MW; 7A5F5DD66A96FDD3 CRC64;
MPISAMPGVV QHTLDSLVAE AERCVAAGVG GLMVFGVPVE KDPRGSGADD PDGILNVALR
RLRDAVGDDL VLVADLCLDE FTSHGHCGVL APDGSVDNDA TLVRYAEMGL AQAEAGAHVL
GLSGMMDGQV GFVREALDEE GLIDTVLLAY AAKYTSGLYG PFREAVGSSL VGDRATYQQD
PPNATEAVRE IELDLAEGAD IVMVKPAGPN LDIVAAAADL SPVPVAAYQI SGEYAQIEAA
AANGWIDRDR VMAESLIGIK RAGAQIIATY YALEMARHLR
//
