ID G4NN11_CHLT4 Unreviewed; 342 AA.
AC G4NN11;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=CTO_0687 {ECO:0000313|EMBL:AEP35509.1};
OS Chlamydia trachomatis serovar A (strain A2497).
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=580047 {ECO:0000313|EMBL:AEP35509.1, ECO:0000313|Proteomes:UP000009287};
RN [1] {ECO:0000313|EMBL:AEP35509.1, ECO:0000313|Proteomes:UP000009287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2497 {ECO:0000313|EMBL:AEP35509.1,
RC ECO:0000313|Proteomes:UP000009287};
RX PubMed=21987657; DOI=10.1084/jem.20111266;
RA Kari L., Whitmire W.M., Olivares-Zavaleta N., Goheen M.M., Taylor L.D.,
RA Carlson J.H., Sturdevant G.L., Lu C., Bakios L.E., Randall L.B.,
RA Parnell M.J., Zhong G., Caldwell H.D.;
RT "A live-attenuated chlamydial vaccine protects against trachoma in nonhuman
RT primates.";
RL J. Exp. Med. 208:2217-2223(2011).
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; CP002401; AEP35509.1; -; Genomic_DNA.
DR AlphaFoldDB; G4NN11; -.
DR KEGG; cra:CTO_0687; -.
DR PATRIC; fig|580047.4.peg.699; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000009287; 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}.
FT ACT_SITE 203
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 256
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ SEQUENCE 342 AA; 38268 MW; B7B31C99A2A77CAA CRC64;
MYNFMTRLPL LKRPRRNRKS AAVRSIIQET QLCSSDLIWP IFLKDGSGIR EEIKSMPGVY
RWSLDMVSKE LERLCTIGLK AVTLFPVIDA NKKEQFGSYA SHPYNIVCKG IQAIKKSFPE
LCVISDIALD PFTTSGHDGI FHNNYVINDE SVRVYGGIAV MHAEMGADIV APSDMMDGRV
KHIREQMDQM GFVNTGILSY SAKYASALYG PFRDALSSHL QSGDKRTYQM DPANVQEALL
ECQLDEEEGA DMVMIKPAGF YLDVIVKARE NTHLPVVAYQ VSGEFSMIMA ACLHGWLNKE
SVIKESLLAI KRAGATAIIS YATPWVLEWL AKDALPFERS VL
//
