ID   HEM1_CANAL              Reviewed;         564 AA.
AC   O94069; Q5A965;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=5-aminolevulinate synthase, mitochondrial;
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;
DE   Flags: Precursor;
GN   Name=HEM1; ORFNames=Ca49C4.15, CaO19.2601;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1161;
RA   Murphy L., Harris D., Barrell B.G., Rajandream M.A.;
RT   "Candida albicans strain 1161 genome pilot sequencing project.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
RA   Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
RA   Davis R.W., Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
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   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family.
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DR   EMBL; AL033503; CAA22025.1; -; Genomic_DNA.
DR   EMBL; AACQ01000044; EAK99337.1; -; Genomic_DNA.
DR   PIR; T18251; T18251.
DR   RefSeq; XP_718266.1; -.
DR   HSSP; P07912; 1FC4.
DR   GeneID; 3640149; -.
DR   CGD; CAL0003351; HEM1.
DR   BRENDA; 2.3.1.37; 1124.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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; Heme biosynthesis; Mitochondrion;
KW   Pyridoxal phosphate; Transferase; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion.
FT   CHAIN         ?    564       5-aminolevulinate synthase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000001237.
FT   MOD_RES     353    353       N6-(pyridoxal phosphate)lysine
FT                                (Probable).
SQ   SEQUENCE   564 AA;  61395 MW;  C984334068F40487 CRC64;
     MESITKVSMS VCPFVRSTST QALRQLSQTS GALANQARQC PIAGNAIRAK EISIRSYSSA
     TKPVRATAAT PSTPEATFNV SSSFELGSKE TAFDYNGYLG NELEKKRSDK SYRYFNNINR
     LANEFPKAHR TQEEDKVTVW CSNDYLGMGK NENTLKEMKR VLDKYGSGAG GTRNIAGHNS
     HAIKLESELA ALHKHDAALV FSSCFVANDA VLSLLGQKIK DLVIFSDELN HASMIQGIRN
     SRARKHIFKH NNLADLESKL AQYPKSTPKL IAFESVYSMC GSIAPIEAIC DLAEKYGALT
     FLDEVHAVGM YGPHGAGVAE HLNFEAHLKS GIERPEITTV MSRVDMVTGT LGKAYGVVGG
     YITGKTNLID WFRSYAPGFI FTTSLPPAIM AGCSASIRYQ RATLKDRIAQ QKNTRLVKNN
     LNELGIPVIP NPSHIVPVLV GNAADAKRAS DLLLNKHDIY VQAINFPTVP IGEERLRITP
     TPGHGPELSK QLVEAVDSVF TELNLNRIND WKKLGGLVGV GVEGAAKVEH IWTEEQLALT
     DADLNPNVVN PAISPLDVSS GIST
//