HEM1_BRADU
ID HEM1_BRADU Reviewed; 409 AA.
AC P08262;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=5-aminolevulinate synthase;
DE EC=2.3.1.37;
DE AltName: Full=5-aminolevulinic acid synthase;
DE AltName: Full=Delta-ALA synthase;
DE AltName: Full=Delta-aminolevulinate synthase;
GN Name=hemA; OrderedLocusNames=bll1200;
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].
RX PubMed=3609750; DOI=10.1016/0378-1119(87)90355-6;
RA McClung C.R., Somerville J.E., Guerinot M.L., Chelm B.K.;
RT "Structure of the Bradyrhizobium japonicum gene hemA encoding 5-
RT aminolevulinic acid synthase.";
RL Gene 54:133-139(1987).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA;
CC Xref=Rhea:RHEA:12921, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:356416; EC=2.3.1.37;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P18079};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from glycine: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P18079}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; M16751; AAA26216.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC46465.1; -; Genomic_DNA.
DR PIR; A27478; SYZJAL.
DR RefSeq; NP_767840.1; NC_004463.1.
DR RefSeq; WP_011084018.1; NZ_CP011360.1.
DR AlphaFoldDB; P08262; -.
DR SMR; P08262; -.
DR STRING; 224911.27349451; -.
DR EnsemblBacteria; BAC46465; BAC46465; BAC46465.
DR GeneID; 64021069; -.
DR KEGG; bja:bll1200; -.
DR PATRIC; fig|224911.44.peg.602; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_1_5; -.
DR InParanoid; P08262; -.
DR OMA; HRIDIFN; -.
DR PhylomeDB; P08262; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0003870; F:5-aminolevulinate synthase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR010961; 4pyrrol_synth_NH2levulA_synth.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01821; 5aminolev_synth; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Heme biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..409
FT /note="5-aminolevulinate synthase"
FT /id="PRO_0000163825"
FT ACT_SITE 247
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 188
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 216
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 244
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 276
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 277
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT MOD_RES 247
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT CONFLICT 261
FT /note="Q -> R (in Ref. 1; AAA26216)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 44574 MW; B21B011EB9542D66 CRC64;
MDYSQFFNSA LDRLHTERRY RVFADLERMA GRFPHAIWHS PKGKRDVVIW CSNDYLGMGQ
HPKVVGAMVE TATRVGTGAG GTRNIAGTHH PLVQLEAELA DLHGKEAALL FTSGYVSNQT
GIATIAKLIP NCLILSDELN HNSMIEGIRQ SGCERQVFRH NDLADLEALL KAAGANRPKL
IACESLYSMD GDVAPLAKIC DLAEKYNAMT YVDEVHAVGM YGPRGGGIAE RDGVMHRIDI
LEGTLAKAFG CLGGYIAANG QIIDAVRSYA PGFIFTTALP PAICSAATAA IKHLKTSSWE
RERHQDRAAR VKAILNAAGL PVMSSDTHIV PLFIGDAEKC KQASDLLLEE HGIYIQPINY
PTVAKGSERL RITPSPYHDD GLIDQLAEAL LQVWDRLGLP LKQKSLAAE
