ID I4AN39_BERLS Unreviewed; 331 AA.
AC I4AN39;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
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 OrderedLocusNames=Fleli_3033 {ECO:0000313|EMBL:AFM05374.1};
OS Bernardetia litoralis (strain ATCC 23117 / DSM 6794 / NBRC 15988 / NCIMB
OS 1366 / Fx l1 / Sio-4) (Flexibacter litoralis).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Bernardetiaceae;
OC Bernardetia.
OX NCBI_TaxID=880071 {ECO:0000313|EMBL:AFM05374.1, ECO:0000313|Proteomes:UP000006054};
RN [1] {ECO:0000313|Proteomes:UP000006054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23117 / DSM 6794 / NBRC 15988 / NCIMB 1366 / Sio-4
RC {ECO:0000313|Proteomes:UP000006054};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Lang E., Kopitz M., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "The complete genome of Flexibacter litoralis DSM 6794.";
RL Submitted (JUN-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}.
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DR EMBL; CP003345; AFM05374.1; -; Genomic_DNA.
DR RefSeq; WP_014798806.1; NC_018018.1.
DR AlphaFoldDB; I4AN39; -.
DR STRING; 880071.Fleli_3033; -.
DR KEGG; fli:Fleli_3033; -.
DR PATRIC; fig|880071.3.peg.3030; -.
DR eggNOG; COG0113; Bacteria.
DR HOGENOM; CLU_035731_0_0_10; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000006054; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006054}.
FT ACT_SITE 201
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 254
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ SEQUENCE 331 AA; 37053 MW; FF45DFD423F301E3 CRC64;
MSFDFQSMRS RPRRNRQSAV IRAMVEETSL SISDFMFPVF VMEGTNKKEP IASMPNIFRY
SLDRLLEEIE ECYKLGIRAF APFPSLTDEY KDAMATSSHN PENIYLKAIT AIKEKFPDVF
IMTDIAMDPY SSDGHDGIYK DGKILNDETL EVLGKMAVAQ ARAGADYVGP SDMMDGRVAY
LRHALDKEGF QDVGIIAYTA KYASAFYGPF RDALDSEPRF GDKKTYQMNP ANVREALLEA
KLDIEEGADM IMVKPALSYL DVISKLNQNS NIPIVAYNVS GEYAIVKAGA EKGWIDGEKI
MLETLLSIKR AGAKIILSYF AKEVAQILSK K
//
