ID   HEM1_RHIME              Reviewed;         404 AA.
AC   P08080;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 2.
DT   16-JUN-2009, entry version 78.
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=R02989; ORFNames=SMc03104;
OS   Rhizobium meliloti (Sinorhizobium meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   MEDLINE=21396507; PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D.,
RA   Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U.,
RA   Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont
RT   Sinorhizobium meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74.
RX   MEDLINE=85297790; PubMed=2994020; DOI=10.1093/nar/13.16.5965;
RA   Leong S.A., Williams P.H., Ditta G.S.;
RT   "Analysis of the 5' regulatory region of the gene for delta-
RT   aminolevulinic acid synthetase of Rhizobium meliloti.";
RL   Nucleic Acids Res. 13:5965-5976(1985).
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; AL591688; CAC47568.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X02853; CAA26610.1; ALT_INIT; Genomic_DNA.
DR   PIR; A24077; A24077.
DR   RefSeq; NP_387095.1; -.
DR   HSSP; P07912; 1FC4.
DR   GeneID; 1234673; -.
DR   GenomeReviews; AL591688_GR; R02989.
DR   KEGG; sme:SMc03104; -.
DR   NMPDR; fig|266834.1.peg.4283; -.
DR   HOGENOM; P08080; -.
DR   OMA; P08080; FSPIKDI.
DR   BioCyc; SMEL266834:SMC03104-MON; -.
DR   BRENDA; 2.3.1.37; 142.
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    404       5-aminolevulinate synthase.
FT                                /FTId=PRO_0000163827.
FT   MOD_RES     247    247       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   404 AA;  44116 MW;  826BC15187083E07 CRC64;
     MDFESFFKNE LDGLHQEGRY RVFADLARHR GSFPKATRYT ADGAQEVTVW CSNDYLGMGQ
     CPIVTEAMKN AIDECGAGAG GTRNISGTNH YHVLLERELA DLHGKESALL FTSGYVSNWA
     ALGTLCSKIP GVIVFSDAGN HASMIEGIRH SKCERVIFKH NSVADLEAKL AAADPRAPKI
     IAFESVYSMD GDIAPIREFC DLADKYGAMT YLDEVHAVGM YGPRGGGIAE REGLMHRLTV
     IEGTLGKAFG VMGGYITGSA ALCDFIRSFA SGFIFTTALP PALAAGALAS IRHLKESQVE
     RFAHQERVRR LRSLLDQRGI PHMVNPSHIV PVIVGDAAKC KWISDLLLDN FGIYVQPINY
     PTVPKKTERL RITPTPMHSD ADIDHLVSAL HSLWSRCALA RAVA
//