ID   HEM1_BRAJA              Reviewed;         409 AA.
AC   P08262;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2003, sequence version 2.
DT   16-JUN-2009, entry version 73.
DE   RecName: Full=5-aminolevulinate synthase;
DE            EC=2.3.1.37;
DE   AltName: Full=5-aminolevulinic acid synthase;
DE   AltName: Full=Delta-aminolevulinate synthase;
DE   AltName: Full=Delta-ALA synthetase;
GN   Name=hemA; OrderedLocusNames=bll1200;
OS   Bradyrhizobium japonicum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=87277426; 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=USDA 110;
RX   MEDLINE=22484998; PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T.,
RA   Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K.,
RA   Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M.,
RA   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: Succinyl-CoA + glycine = 5-aminolevulinate +
CC       CoA + CO(2).
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-
CC       aminolevulinate from glycine: step 1/1.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family.
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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; -.
DR   HSSP; P07912; 1FC4.
DR   GeneID; 1049580; -.
DR   GenomeReviews; BA000040_GR; bll1200.
DR   KEGG; bja:bll1200; -.
DR   NMPDR; fig|224911.1.peg.1200; -.
DR   HOGENOM; P08262; -.
DR   OMA; P08262; AMCETAG.
DR   BioCyc; BJAP224911:BLL1200-MON; -.
DR   BRENDA; 2.3.1.37; 280.
DR   GO; GO:0003870; F:5-aminolevulinate synthase activity; IEA:EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016769; F:transferase activity, transferring nitrogen...; IEA:InterPro.
DR   GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR010961; 4pyrrol_synth_NH2levulA_synth.
DR   InterPro; IPR004839; Aminotrans_I/II.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   TIGRFAMs; TIGR01821; 5aminolev_synth; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Complete proteome; Heme biosynthesis;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN         1    409       5-aminolevulinate synthase.
FT                                /FTId=PRO_0000163825.
FT   MOD_RES     247    247       N6-(pyridoxal phosphate)lysine
FT                                (Probable).
FT   CONFLICT    261    261       Q -> R (in Ref. 1; AAA26216).
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
//