ID A0A0R2UFC2_9GAMM Unreviewed; 330 AA.
AC A0A0R2UFC2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 03-MAY-2023, 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=ABS10_04675 {ECO:0000313|EMBL:KRO96051.1};
OS SAR86 cluster bacterium BACL1 MAG-120820-bin45.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; SAR86 cluster.
OX NCBI_TaxID=1655612 {ECO:0000313|EMBL:KRO96051.1, ECO:0000313|Proteomes:UP000051027};
RN [1] {ECO:0000313|EMBL:KRO96051.1, ECO:0000313|Proteomes:UP000051027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL1 MAG-120820-bin45 {ECO:0000313|EMBL:KRO96051.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) 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:KRO96051.1}.
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DR EMBL; LICS01000008; KRO96051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2UFC2; -.
DR STRING; 1655612.ABS10_04675; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000051027; 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 200
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 255
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ SEQUENCE 330 AA; 36393 MW; 4F543A17F92273CA CRC64;
MINRNFPSTR LRRTRAKSFL RDLVAENKLS SDDLIQPIFV ADQKESQVDI PSMPGIFRHN
LDSLYSEAEA LLNAGVKSIA IFPAIDPDKK NAEASHAFDS DNIICKALQG INERFPEIVT
IADVALDPYT DHGHDGLLIN EKIDNDRTLT LLSKQALLLA EAGADIIAPS DMMDGRVKII
REALEANQFN DTVILSYAAK YASSFYGPFR DAVGSSTSLG KGSKKTYQMN FANTQEAMHE
VAMDIQEGAD IVMIKPGTAY LDIVQKIKLQ FQVPTFVYQV SGEYSMLTLS IEKGWLDKNV
MLESLVCCKR AGADAILTYA AKQIASELNS
//
