HEM2_CHLP8
ID HEM2_CHLP8 Reviewed; 328 AA.
AC Q59334; B3QMJ8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Delta-aminolevulinic acid dehydratase;
DE Short=ALAD;
DE Short=ALADH;
DE EC=4.2.1.24;
DE AltName: Full=Porphobilinogen synthase;
GN Name=hemB; OrderedLocusNames=Cpar_0732;
OS Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme
OS subsp. thiosulfatophilum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=517417;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8626508; DOI=10.1074/jbc.271.14.8176;
RA Rhie G.-E., Avissar Y.J., Beale S.I.;
RT "Structure and expression of the Chlorobium vibrioforme hemB gene and
RT characterization of its encoded enzyme, porphobilinogen synthase.";
RL J. Biol. Chem. 271:8176-8182(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 263 / NCIMB 8327;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobaculum parvum NCIB 8327.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP LAEVULINIC ACID, ACTIVE SITE, AND SUBUNIT.
RX PubMed=15327955; DOI=10.1016/j.jmb.2004.07.007;
RA Coates L., Beaven G., Erskine P.T., Beale S.I., Avissar Y.J., Gill R.,
RA Mohammed F., Wood S.P., Shoolingin-Jordan P., Cooper J.B.;
RT "The X-ray structure of the plant like 5-aminolaevulinic acid dehydratase
RT from Chlorobium vibrioforme complexed with the inhibitor laevulinic acid at
RT 2.6 A resolution.";
RL J. Mol. Biol. 342:563-570(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP 4,7-DIOXOSEBACIC ACID, AND ACTIVE SITE.
RX PubMed=16304458; DOI=10.1107/s0907444905030350;
RA Coates L., Beaven G., Erskine P.T., Beale S.I., Wood S.P.,
RA Shoolingin-Jordan P.M., Cooper J.B.;
RT "Structure of Chlorobium vibrioforme 5-aminolaevulinic acid dehydratase
RT complexed with a diacid inhibitor.";
RL Acta Crystallogr. D 61:1594-1598(2005).
CC -!- FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles.
CC Binds two molecules of 5-aminolevulinate per subunit, each at a
CC distinct site, and catalyzes their condensation to form
CC porphobilinogen.
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 -!- ACTIVITY REGULATION: Stimulated by magnesium, inhibited by zinc.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:15327955,
CC ECO:0000269|PubMed:16304458}.
CC -!- MISCELLANEOUS: Does not seem to have a metal requirement for activity.
CC {ECO:0000269|PubMed:15327955}.
CC -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000305}.
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DR EMBL; U38348; AAC43975.1; -; Genomic_DNA.
DR EMBL; CP001099; ACF11151.1; -; Genomic_DNA.
DR RefSeq; WP_012501984.1; NC_011027.1.
DR PDB; 1W1Z; X-ray; 2.60 A; A/B=1-328.
DR PDB; 2C1H; X-ray; 2.60 A; A/B=1-328.
DR PDBsum; 1W1Z; -.
DR PDBsum; 2C1H; -.
DR AlphaFoldDB; Q59334; -.
DR SMR; Q59334; -.
DR STRING; 517417.Cpar_0732; -.
DR DrugBank; DB04560; 4,7-Dioxosebacic Acid.
DR EnsemblBacteria; ACF11151; ACF11151; Cpar_0732.
DR KEGG; cpc:Cpar_0732; -.
DR eggNOG; COG0113; Bacteria.
DR HOGENOM; CLU_035731_0_0_10; -.
DR OMA; YQMDYAN; -.
DR OrthoDB; 677575at2; -.
DR UniPathway; UPA00251; UER00318.
DR EvolutionaryTrace; Q59334; -.
DR Proteomes; UP000008811; 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; -; 1.
DR InterPro; IPR001731; ALAD.
DR InterPro; IPR030656; ALAD_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR PANTHER; PTHR11458; PTHR11458; 1.
DR Pfam; PF00490; ALAD; 1.
DR PIRSF; PIRSF001415; Porphbilin_synth; 1.
DR PRINTS; PR00144; DALDHYDRTASE.
DR SMART; SM01004; ALAD; 1.
DR PROSITE; PS00169; D_ALA_DEHYDRATASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme biosynthesis; Lyase; Magnesium; Metal-binding;
KW Porphyrin biosynthesis.
FT CHAIN 1..328
FT /note="Delta-aminolevulinic acid dehydratase"
FT /id="PRO_0000140499"
FT ACT_SITE 200
FT /note="Schiff-base intermediate with substrate"
FT ACT_SITE 253
FT /note="Schiff-base intermediate with substrate"
FT BINDING 210
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT BINDING 222
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15327955,
FT ECO:0000269|PubMed:16304458"
FT BINDING 279
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT BINDING 318
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:1W1Z"
FT HELIX 20..26
FT /evidence="ECO:0007829|PDB:1W1Z"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:1W1Z"
FT STRAND 36..47
FT /evidence="ECO:0007829|PDB:1W1Z"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1W1Z"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:1W1Z"
FT HELIX 63..75
FT /evidence="ECO:0007829|PDB:1W1Z"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1W1Z"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:1W1Z"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:1W1Z"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:1W1Z"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:1W1Z"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:1W1Z"
FT HELIX 145..162
FT /evidence="ECO:0007829|PDB:1W1Z"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:1W1Z"
FT HELIX 176..186
FT /evidence="ECO:0007829|PDB:1W1Z"
FT STRAND 192..201
FT /evidence="ECO:0007829|PDB:1W1Z"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:1W1Z"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:1W1Z"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:1W1Z"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:1W1Z"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1W1Z"
FT HELIX 259..269
FT /evidence="ECO:0007829|PDB:1W1Z"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:1W1Z"
FT HELIX 279..290
FT /evidence="ECO:0007829|PDB:1W1Z"
FT HELIX 296..310
FT /evidence="ECO:0007829|PDB:1W1Z"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:1W1Z"
FT HELIX 320..327
FT /evidence="ECO:0007829|PDB:1W1Z"
SQ SEQUENCE 328 AA; 36395 MW; D31B234328ABBE7B CRC64;
MSQLDLLNIV HRPRRLRRTA ALRNLVQENT LTVNDLVFPL FVMPGTNAVE EVSSMPGSFR
FTIDRAVEEC KELYDLGIQG IDLFGIPEQK TEDGSEAYND NGILQQAIRA IKKAVPELCI
MTDVALDPFT PFGHDGLVKD GIILNDETVE VLQKMAVSHA EAGADFVSPS DMMDGRIGAI
REALDETDHS DVGILSYAAK YASSFYGPFR DALHSAPQFG DKSTYQMNPA NTEEAMKEVE
LDIVEGADIV MVKPGLAYLD IVWRTKERFD VPVAIYHVSG EYAMVKAAAA KGWIDEDRVM
MESLLCMKRA GADIIFTYYA KEAAKKLR
