ID   HEM1_RICFE              Reviewed;         414 AA.
AC   Q4UJV4;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
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=RF_1334;
OS   Rickettsia felis (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=42862;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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; CP000053; AAY62185.1; -; Genomic_DNA.
DR   RefSeq; YP_247350.1; -.
DR   GeneID; 3400890; -.
DR   GenomeReviews; CP000053_GR; RF_1334.
DR   KEGG; rfe:RF_1334; -.
DR   NMPDR; fig|315456.3.peg.1334; -.
DR   HOGENOM; Q4UJV4; -.
DR   OMA; Q4UJV4; FSPIKDI.
DR   BioCyc; RFEL315456:RF_1334-MON; -.
DR   BRENDA; 2.3.1.37; 297363.
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_0000280898.
FT   MOD_RES     244    244       N6-(pyridoxal phosphate)lysine
FT                                (Probable).
SQ   SEQUENCE   414 AA;  46180 MW;  6B7987FD78DEF8AB CRC64;
     MSYYDTIFSK HIDKIKSEGR YREFKALKRQ ADNFPFAEHA NKQIVMWCIN DYLGMSKHAK
     VMQASIDALL KYGVGSGGTR NIGGNNIAIL ELEKELADLH KKQAALVFTS GFVANDTTLA
     SLAKIMPDIV FFSDELNHAS IIAGVTSSRA EKYIYRHLDV KHLEELLQSV DINRPKIIVF
     ESAYSMDGFF SPIKDIINLA KKYNALTFID EVHTVGLYGK HGGGIAELLN CSDQIDIIQG
     TLAKAYGTIG GYITSNHNLV DAIRLTAPGF IFTTSLPPVI STAATHSIRH LKESNEERIK
     HQEVVTKLKN SFENFNIPYL KNESHIVPII IGDPIKAASA SNMLLNKYGI YVQHINFPTV
     PRGTERLRII PTPAHTDKMI NDLSIALVHI FAELDIELSS TKELNEEIRL NLIA
//