ID   HEM1_AGABI              Reviewed;         621 AA.
AC   Q92403;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   16-JUN-2009, entry version 56.
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;
OS   Agaricus bisporus (Common mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Homobasidiomycetes; Agaricomycetidae; Agaricales; Agaricaceae;
OC   Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=D649;
RA   Yague E., Mehak-Zunic M., Wood D.A., Thurston C.F.;
RL   Submitted (NOV-1996) 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   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family.
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DR   EMBL; Z50096; CAA90424.1; -; mRNA.
DR   HSSP; P07912; 1FC4.
DR   BRENDA; 2.3.1.37; 984.
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   2: Evidence at transcript level;
KW   Acyltransferase; Heme biosynthesis; Mitochondrion;
KW   Pyridoxal phosphate; Transferase; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion.
FT   CHAIN         ?    621       5-aminolevulinate synthase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000001235.
FT   MOD_RES     362    362       N6-(pyridoxal phosphate)lysine
FT                                (Probable).
SQ   SEQUENCE   621 AA;  67426 MW;  A335C3268FAE1AA3 CRC64;
     MSHHGPRLST RSQQIVAGYA SVAANFDVEK LHREQGVNIP TSGASINQCP HAAAARAAAR
     MADDLASAAR AKKSLDAKGS LAGRPVHHKA ATESTKAKHT GFDYEAFYKG ELAKKHQDKS
     YRYFNNINRL ARKFPVAHTA NPRDEVEVWC SNDYLGMGNN PVVLETMHRT LDKYGHGAGG
     TRNIAGNGAM HLGLERELRL HRKEAALVFS SCYVANDATL STLGTKLPGC VIFSDTMNHA
     SMIQGMRHST PKRVIFKHND LEDLETKLQQ YPKETPKIIA FESVYSMCGS IGPVKEICDL
     AEQYGAITFL DEVHAVGLYG PRGAGVAEHL DYDAHLAAGS SPDPIPGSVM DRIDIITGTL
     GKSYGAVGGY IAGSEEFVDM IRSYAPGFIF TTSLPPATVA GARASIVYQS EYLGDRQLKQ
     INVREVKRRL AELDIPVVPG SSHIVPVLVG DAALARAASD KLLSEHDIYV QAINYPTVAR
     GEERLRITVT PRHTMEQMEG LIRSLNQVFE ELNINRLSDW KLAGGRAGVG IPGAADDVQP
     IWTDEQIGLL NGTAPRSLRN AEKSVVDMRA VTIARSRFDV LLGPVYGELQ PTEDFDTPAV
     GATFKAPLVD REVAHDITVS A
//