ID   U7GFL4_9GAMM            Unreviewed;       337 AA.
AC   U7GFL4;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=Q674_04105 {ECO:0000313|EMBL:ERP97005.1};
OS   Acinetobacter sp. COS3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1397525 {ECO:0000313|EMBL:ERP97005.1, ECO:0000313|Proteomes:UP000018430};
RN   [1] {ECO:0000313|EMBL:ERP97005.1, ECO:0000313|Proteomes:UP000018430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COS3 {ECO:0000313|EMBL:ERP97005.1,
RC   ECO:0000313|Proteomes:UP000018430};
RX   PubMed=24356826;
RA   Overholt W.A., Green S.J., Marks K.P., Venkatraman R., Prakash O.,
RA   Kostka J.E.;
RT   "Draft genome sequences for oil-degrading bacterial strains from beach
RT   sands impacted by the deepwater horizon oil spill.";
RL   Genome Announc. 1:e01015-13(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         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:ERP97005.1}.
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DR   EMBL; AXCD01000056; ERP97005.1; -; Genomic_DNA.
DR   RefSeq; WP_007481269.1; NZ_AXCD01000056.1.
DR   AlphaFoldDB; U7GFL4; -.
DR   PATRIC; fig|1397525.3.peg.2555; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000018430; 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        205
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   ACT_SITE        260
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   BINDING         245
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ   SEQUENCE   337 AA;  37252 MW;  375EF20862CB0F76 CRC64;
     MTYTFNRPAF PATRMRRIRK NDQLRAMVSE TQLTANHLIY PVFVLPGQQQ TQDIPSMPNV
     QRLSADLLLK KAESLLELGV SKLALFPVTP QEDKSLTAEA AWDENGLVQT TCRLLKKELP
     EMVLITDGAL DPYTTHGQDG IIDDTGYVLN DETVECLVKQ ALSHAAAGAD VVAPSDMMDG
     RIGAIRQALE QNNFIYTNIM AYSAKYASSF YGPFRDAVGS ASNLKGGNKY NYQMDVGNRA
     EALHEIALDI QEGADMVIVK PGMPYLDIVR EVKDTFGVPT FIYQVSGEYA MLAGAIQNGW
     LSESVILESL MCCRRAGADG IWTYFAEDAA RKLKEMK
//