GenomeNet

Database: UniProt
Entry: I3ZZF8_ORNRL
LinkDB: I3ZZF8_ORNRL
Original site: I3ZZF8_ORNRL 
ID   I3ZZF8_ORNRL            Unreviewed;       326 AA.
AC   I3ZZF8;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
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=Ornrh_0897 {ECO:0000313|EMBL:AFL97092.1};
OS   Ornithobacterium rhinotracheale (strain ATCC 51463 / DSM 15997 / CCUG 23171
OS   / CIP 104009 / LMG 9086).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Ornithobacterium.
OX   NCBI_TaxID=867902 {ECO:0000313|EMBL:AFL97092.1, ECO:0000313|Proteomes:UP000006051};
RN   [1] {ECO:0000313|EMBL:AFL97092.1, ECO:0000313|Proteomes:UP000006051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51463 / DSM 15997 / CCUG 23171 / LMG 9086
RC   {ECO:0000313|Proteomes:UP000006051};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA   Mikhailova N., Teshima H., Kyrpides N., Mavromatis K., Pagani I.,
RA   Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Lang E., Kopitz M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Ornithobacterium rhinotracheale DSM 15997.";
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003283; AFL97092.1; -; Genomic_DNA.
DR   RefSeq; WP_014790693.1; NC_018016.1.
DR   AlphaFoldDB; I3ZZF8; -.
DR   STRING; 867902.Ornrh_0897; -.
DR   GeneID; 71569186; -.
DR   KEGG; orh:Ornrh_0897; -.
DR   PATRIC; fig|867902.3.peg.879; -.
DR   eggNOG; COG0113; Bacteria.
DR   HOGENOM; CLU_035731_0_0_10; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000006051; 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:UP000006051}.
FT   ACT_SITE        196
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   ACT_SITE        249
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT   BINDING         234
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ   SEQUENCE   326 AA;  36931 MW;  AD340E63B54FC60C CRC64;
     MYPYQRNRRT RSNEAIRNIV RETSLSTHDL MLPLFIMEGE NLREEIPSMP GVYRITLDVL
     EKEIQEIWDL GIQAVNIYCK VPDELKDNEG TEALNPNGLM QRAIKTIKKA QKDMLVFTDV
     ALDPVSSYGH DGIVENGEIL NDETVEILAK MALSHAEAGA DFIAPSDMMD GRVLAIREIL
     EQNGFHNVGI MSYTAKYASS FYGPFRDALD SAPGFGDKKT YQMDYANVQE AYREADNDLI
     EGADILMVKP GMPYLDVLYR MKEYTKMPIA VYQVSGEYAM LKAAAEKGWL DFEKCLMESM
     YAFKRAGADL INTYYAKEVA TILNRK
//
DBGET integrated database retrieval system