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   27-MAR-2024, entry version 144.
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; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; 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.AAV28_02880; -.
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   OrthoDB; 9807157at2; -.
DR   PhylomeDB; P08262; -.
DR   UniPathway; UPA00251; UER00375.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0003870; F:5-aminolevulinate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd06454; KBL_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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   NCBIfam; TIGR01821; 5aminolev_synth; 1.
DR   PANTHER; PTHR13693:SF105; 5-AMINOLEVULINATE SYNTHASE; 1.
DR   PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 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
//