ID   HEM1_RICBR              Reviewed;         414 AA.
AC   Q1RIV2;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=RBE_0631;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae
RT   in gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
CC   -!- CATALYTIC ACTIVITY: Succinyl-CoA + glycine = 5-aminolevulinate +
CC       CoA + CO(2).
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
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; CP000087; ABE04712.1; -; Genomic_DNA.
DR   RefSeq; YP_537801.1; -.
DR   GeneID; 3995921; -.
DR   GenomeReviews; CP000087_GR; RBE_0631.
DR   KEGG; rbe:RBE_0631; -.
DR   HOGENOM; Q1RIV2; -.
DR   OMA; Q1RIV2; FSPIKDI.
DR   BioCyc; RBEL336407:RBE_0631-MON; -.
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    414       5-aminolevulinate synthase.
FT                                /FTId=PRO_0000280896.
FT   MOD_RES     244    244       N6-(pyridoxal phosphate)lysine
FT                                (Probable).
SQ   SEQUENCE   414 AA;  45964 MW;  7D110EE50478F213 CRC64;
     MSYYDTIFSD HIDKIKSEGR YREFKALKRQ ADNFPFAMCD DKQIVMWCIN DYLGMSKHPK
     VVQASIDAVL KYGVGSGGTR NIGGNNVAIL ELEQELASLH NKEASLVFTS GFVANDTTLA
     TLAKIMPNIV FFSDELNHAS IIAGITGSKA EKHIYRHLDV KHLEELLQSV DINRPKIIVF
     ESAYSMDGFF SPVKDIINLA KKYNALTFID EVHTVGLYGK TGAGIAELLD CSDEIDIIQG
     TLAKAYGTIG GYITANHSLI DAIRLSASGF IFTTSLPPVI STAATHSIRH LKESNQERKT
     HQQVVSKLKS SFDRFNIPYL KNESHIVPII IGDPIKASKA SNMLLNEYSI YVQHINFPTV
     PRGTERLRII PTPAHTDEMI NDLSIALVQI FAALNIELSS TKELNDEIYL NLIA
//