ID X5HLN3_9RICK Unreviewed; 322 AA.
AC X5HLN3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 03-MAY-2023, entry version 30.
DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|ARBA:ARBA00020771};
DE EC=4.2.1.24 {ECO:0000256|ARBA:ARBA00012053};
DE AltName: Full=Porphobilinogen synthase {ECO:0000256|ARBA:ARBA00032837};
GN ORFNames=NHE_0376 {ECO:0000313|EMBL:AHX11325.1};
OS Neorickettsia helminthoeca str. Oregon.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Neorickettsia.
OX NCBI_TaxID=1286528 {ECO:0000313|EMBL:AHX11325.1, ECO:0000313|Proteomes:UP000023755};
RN [1] {ECO:0000313|EMBL:AHX11325.1, ECO:0000313|Proteomes:UP000023755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon {ECO:0000313|EMBL:AHX11325.1,
RC ECO:0000313|Proteomes:UP000023755};
RA Lin M., Daugherty S.C., Nagaraj S., Cheng Z., Xiong Q., Lin F.-Y.,
RA Sengamalay N., Ott S., Godinez A., Tallon L.J., Sadzewicz L., Fraser C.M.,
RA Dunning Hotopp J.C., Rikihisa Y.;
RT "Sequencing and Comparison of Genomes and Transcriptome Profiles of Human
RT Ehrlichiosis Agents.";
RL Submitted (MAR-2014) 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 -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004694}.
CC -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000256|ARBA:ARBA00008055,
CC ECO:0000256|RuleBase:RU004161}.
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DR EMBL; CP007481; AHX11325.1; -; Genomic_DNA.
DR RefSeq; WP_038559291.1; NZ_CP007481.1.
DR AlphaFoldDB; X5HLN3; -.
DR STRING; 1286528.NHE_0376; -.
DR KEGG; nhm:NHE_0376; -.
DR HOGENOM; CLU_035731_0_0_5; -.
DR OrthoDB; 9805001at2; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000023755; 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 Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR001731; ALAD.
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.
PE 3: Inferred from homology;
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001415-5};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001415-5};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000023755}.
FT ACT_SITE 199
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 252
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT BINDING 237
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ SEQUENCE 322 AA; 35655 MW; A9CF1357D3E310C5 CRC64;
MITTPFVRLR RIRENPIMRD LVADTFISPS QFIFPVFVVE GENLELSVEE MLGVNVYSID
MLGKVIDRAL SCGVRSFMLF PRVDESKKSD NAEEAYNPDN LICRAVRGLR ERFSSEIVII
TDVAADPYTI SGHDGLLQNG KILNDETLEL LAKQALVQVA AGSDMIAPSD MMDGRILAIR
NALDLGNLSS VPILSYSVKY ASKLYKPFRS AIGVNKGPID KRSYQVDCRN SGEAMREIEV
DIAEGADIVM IKPANLFLDV IGKAVDQFSV PIFAYQVSGE YQMFRQYGGI EMLIESLIGI
KRAGVSSICT YAAIEVAEYL KP
//
