ID   HEM1_RICCN              Reviewed;         414 AA.
AC   Q92G23;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   16-JUN-2009, entry version 45.
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=RC1303;
OS   Rickettsia conorii.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=781;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   MEDLINE=21442074; PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M.,
RA   Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL03841.1; ALT_INIT; Genomic_DNA.
DR   PIR; G97862; G97862.
DR   RefSeq; NP_360940.1; -.
DR   GeneID; 928451; -.
DR   GenomeReviews; AE006914_GR; RC1303.
DR   KEGG; rco:RC1303; -.
DR   NMPDR; fig|272944.1.peg.1303; -.
DR   HOGENOM; Q92G23; -.
DR   BioCyc; RCON272944:RC1303-MON; -.
DR   BRENDA; 2.3.1.37; 267518.
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_0000280897.
FT   MOD_RES     244    244       N6-(pyridoxal phosphate)lysine
FT                                (Probable).
SQ   SEQUENCE   414 AA;  46238 MW;  D6E5838194CE8504 CRC64;
     MSYYDIIFSK HIDKIKSEGR YREFKALKRQ ADNFPFAEHA NKQIVMWCIN DYLGMSKHAK
     VMHASIDALL KYGVGSGGTR NIGGNNIAIL ELEKELANLH KKQAALVFTS GFVANDTTLA
     SLAKIMPDIV FFSDELNHAS IIAGITSSRA EKYIYRHLDV KHLEELLQSV DINRPKIVVF
     ESAYSMDGFF SPIKDIINLA KKYNALTFID EVHTVGLYGK QGGGIAELLN CSDQIDIIQG
     TLAKAYGTIG GYITSNHNLV DAIRLTAPGF IFTTSLPPVI STAATHSIRH LKESNEERIK
     HQEVVTKLKN SFERFNIPYL KNESHIVPII IGDPIKTAKA SNMLLNEYGI YVQHINFPTV
     PRGTERLRII PTPAHTDKMI NDLSVALVQI FAELDIELSS AKELNEEVRL NLIA
//