HEM2_BRADU
ID HEM2_BRADU Reviewed; 353 AA.
AC P45622;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, 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=blr5037;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, FUNCTION, AND
RP COFACTOR.
RC STRAIN=I110;
RX PubMed=8226669; DOI=10.1128/jb.175.22.7222-7227.1993;
RA Chauhan S., O'Brian M.R.;
RT "Bradyrhizobium japonicum delta-aminolevulinic acid dehydratase is
RT essential for symbiosis with soybean and contains a novel metal-binding
RT domain.";
RL J. Bacteriol. 175:7222-7227(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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. Required for nodule development.
CC {ECO:0000269|PubMed:8226669}.
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:0000269|PubMed:8226669};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8226669};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC -!- SUBUNIT: Homooctamer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC50302.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L24386; AAA89067.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC50302.1; ALT_INIT; Genomic_DNA.
DR PIR; A49925; A49925.
DR RefSeq; NP_771677.2; NC_004463.1.
DR RefSeq; WP_038966342.1; NZ_CP011360.1.
DR AlphaFoldDB; P45622; -.
DR SMR; P45622; -.
DR STRING; 224911.27353302; -.
DR EnsemblBacteria; BAC50302; BAC50302; BAC50302.
DR GeneID; 64024800; -.
DR KEGG; bja:blr5037; -.
DR PATRIC; fig|224911.44.peg.4902; -.
DR eggNOG; COG0113; Bacteria.
DR HOGENOM; CLU_470668_0_0_5; -.
DR InParanoid; P45622; -.
DR OMA; YQMDYAN; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004655; F:porphobilinogen synthase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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 Heme biosynthesis; Lyase; Magnesium; Metal-binding; Porphyrin biosynthesis;
KW Reference proteome.
FT CHAIN 1..353
FT /note="Delta-aminolevulinic acid dehydratase"
FT /id="PRO_0000140494"
FT ACT_SITE 221
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT ACT_SITE 275
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 353 AA; 38582 MW; F143FA4892ACF1F8 CRC64;
MAIKYGRPIE LREVSRRDGA AASPALDLAI RPRRNRKAEW ARRMVRENVL TTDDLIWPLF
LIDGNNKREQ IASMPGVERL SVDQAVREAE RAMKLTIPCI ALFPYTDPSL RDEEGSEACN
PNNLVCQAVR AIKKEFPEIG VLCDVALDPF TSHGHDGLIA DGAILNDETV AVLVRQALVQ
AEAGCDIIAP SDMMDGRVAA IREGLDQAGL IDVQIMAYAA KYASAFYGPF RDAIGSAKTL
TGDKRTYQMD SANTDEALRE VELDISEGAD MVMVKPGMPY LDVVRRVKDT FAMPTFAYQV
SGEYAMIAAA AGNGWLDGDR AMMESLLAFK RAGADGVLSY FAPKAAEKLR TQG
