ID L9M947_9GAMM Unreviewed; 336 AA.
AC L9M947;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
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 Name=hemB {ECO:0000313|EMBL:ELW83765.1};
GN ORFNames=ACINWC743_1141 {ECO:0000313|EMBL:ELW83765.1};
OS Acinetobacter sp. WC-743.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=903945 {ECO:0000313|EMBL:ELW83765.1, ECO:0000313|Proteomes:UP000011515};
RN [1] {ECO:0000313|EMBL:ELW83765.1, ECO:0000313|Proteomes:UP000011515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WC-743 {ECO:0000313|EMBL:ELW83765.1,
RC ECO:0000313|Proteomes:UP000011515};
RA Harkins D.M., Brinkac L.M., Durkin A.S., Beck E., Fedorova N.B., Kim M.,
RA Onuska J., Radune D., DePew J., Koroleva G.I., Singh I., Chahine M.A.,
RA Cash D.M., Huang X.-Z., Nikolich M.P., Nierman W.C., Fouts D.E.;
RL Submitted (SEP-2012) 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:ELW83765.1}.
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DR EMBL; AMFQ01000079; ELW83765.1; -; Genomic_DNA.
DR AlphaFoldDB; L9M947; -.
DR PATRIC; fig|903945.3.peg.2260; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000011515; 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 336 AA; 37349 MW; 1CC3072A99E9F48D CRC64;
MTYTFNRPAF PATRMRRIRK NDKLRAMVRE TQLTADHLIY PVFVLPGQNQ TQDVPSMPNV
QRLSADLLLK KAETLLELGV SKLALFPVTP QEDKSLTAEA AWHEDGLVQN TLRLLKKELP
EMVLITDGAL DPYTTHGQDG IIDDTGYVLN DETVQCLIKQ ALSHAEAGAD VIAPSDMMDG
RIGAIRQALE SNNFIYTNIM AYSAKYASSF YGPFRDAVGS SSNLKGGNKY NYQMDVGNRA
EALHEIALDI QEGADMVIVK PGMPYLDVVR EVKDTFGVPT FVYQVSGEYA MLAAAIQNGW
LSESVIMESL MCFRRAGADG IWTYYAEDAA RQLKQM
//
