ID   HEM0_RHOS4              Reviewed;         407 AA.
AC   Q06965; Q3IXU1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=5-aminolevulinate synthase 2;
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=hemT; OrderedLocusNames=RHOS4_30750; ORFNames=RSP_3028;
OS   Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM
OS   158).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=93224451; PubMed=8468290;
RA   Neidle E.L., Kaplan S.;
RT   "Expression of the Rhodobacter sphaeroides hemA and hemT genes,
RT   encoding two 5-aminolevulinic acid synthase isozymes.";
RL   J. Bacteriol. 175:2292-2303(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J.,
RA   Kaplan S.;
RT   "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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.
CC   -!- CAUTION: Expressed in the mutant strain HemA1 but expression in
CC       the wild-type strain has not been proven.
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DR   EMBL; L07489; AAA26124.1; -; Genomic_DNA.
DR   EMBL; CP000144; ABA80643.1; -; Genomic_DNA.
DR   PIR; A49845; A49845.
DR   RefSeq; YP_354544.1; -.
DR   HSSP; P07912; 1FC4.
DR   GeneID; 3721613; -.
DR   GenomeReviews; CP000144_GR; RHOS4_30750.
DR   KEGG; rsp:RSP_3028; -.
DR   NMPDR; fig|272943.3.peg.3643; -.
DR   HOGENOM; Q06965; -.
DR   OMA; Q06965; GSRNIGG.
DR   BioCyc; MetaCyc:MON-13234; -.
DR   BioCyc; RSPH272943:RSP_3028-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    407       5-aminolevulinate synthase 2.
FT                                /FTId=PRO_0000163830.
FT   MOD_RES     248    248       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   407 AA;  44333 MW;  4772E3EC1DA55D82 CRC64;
     MEFSQHFQKL IDDMRLDGRY RTFAELERIA GEFPTALWHG PDGQARRVTV WCSNDYLGMG
     QNAEVLAAMH RSIDLSGAGT GGTRNISGTN RQHVALEAEL ADLHGKESAL IFTSGWISNL
     AALGTLGKIL PECAIFSDAL NHNSMIEGIR RSGAERFIFH HNDPVHLDRL LSSVDPARPK
     IVAFESVYSM DGDIAPIAEI CDVAERHGAL TYLDEVHAVG LYGPRGGGIS DRDGLADRVT
     IIEGTLAKAF GVMGGYVSGP SLLMDVIRSM SDSFIFTTSI CPHLAAGALA AVRHVKAHPD
     ERRRQAENAV RLKVLLQKAG LPVLDTPSHI LPVMVGEAHL CRSISEALLA RHAIYVQPIN
     YPTVARGQER FRLTPTPFHT TSHMEALVEA LLAVGRDLGW AMSRRAA
//