ID   HEM1_EMENI              Reviewed;         648 AA.
AC   P38092;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   01-MAY-2007, entry version 45.
DE   5-aminolevulinate synthase, mitochondrial precursor (EC 2.3.1.37) (5-
DE   aminolevulinic acid synthase) (Delta-aminolevulinate synthase) (Delta-
DE   ALA synthetase).
GN   Name=hemA;
OS   Emericella nidulans (Aspergillus nidulans).
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiales; Trichocomaceae; Emericella.
OX   NCBI_TaxID=162425;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=R153;
RX   MEDLINE=93306758; PubMed=8319309; DOI=10.1007/BF00312642;
RA   Bradshaw R.E., Dixon S.W.C., Raitt D.C., Pillar T.M.;
RT   "Isolation and nucleotide sequence of the 5-aminolevulinate synthase
RT   gene from Aspergillus nidulans.";
RL   Curr. Genet. 23:501-507(1993).
CC   -!- CATALYTIC ACTIVITY: Succinyl-CoA + glycine = 5-aminolevulinate +
CC       CoA + CO(2).
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- PATHWAY: Cofactor biosynthesis; porphyrin biosynthesis; 5-
CC       aminolevulinate from glycine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion; mitochondrial matrix.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family.
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DR   EMBL; X64170; CAA45508.1; -; Genomic_DNA.
DR   PIR; S31846; S31846.
DR   HSSP; P07912; 1FC4.
DR   InterPro; IPR010961; 4pyrrol_synth_NH2levulA_synth.
DR   InterPro; IPR004839; Aminotrans_I/II.
DR   InterPro; IPR001917; Aminotrans_II.
DR   Gene3D; G3DSA:3.40.640.10; G3DSA:3.40.640.10; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   TIGRFAMs; TIGR01821; 5aminolev_synth; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
KW   Acyltransferase; Heme biosynthesis; Mitochondrion;
KW   Pyridoxal phosphate; Transferase; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion.
FT   CHAIN         ?    648       5-aminolevulinate synthase.
FT                                /FTId=PRO_0000001240.
FT   BINDING     412    412       Pyridoxal phosphate (covalent) (By
FT                                similarity).
SQ   SEQUENCE   648 AA;  69046 MW;  EC4540EFB7463F56 CRC64;
     MEALLQQSRA MCPFLKRSSP NTLRSLATAT RPSTSPGGGT MTNLQRIARR CPVMSKALAV
     QSARMTGTKR FTSSAAGVPG AGAGTPKPTR GSPGKRALHS TGGNGANMST EFHKGAQQIH
     PGLSNATRSH VGASATVSGP TPRAPVAAPF DYDAFYNAEL QKKHQDKSYR YFNNINRLAQ
     EFPRAHTASK DEKVTVWCSN DYLGMGRNPE VLATMHKTLD TYGAGAGGTR NISGHNQHAV
     SLENTLAKLH GKEAALVFSS CFVANDATLA TLGSKMPDCV ILSDSLNHAS MIQGIRHSGR
     KKMVFKHNDL VDLETKLASL PLHVPKIIAF ESVYSMCGSI APIEAICDLA DKYGAITFLD
     EVHAVGMYGP HGAGVAEHLD YEIYASQDTA NPLSTKGTVM DRINIITGTL GKAYGCVGGY
     IAGSAALVDT IRSLAPGFIF TTSLPPATMA GADTAIRYQA RHQQDRILQQ LHTRAVKQSF
     KDLDIPVIPN PSHIVPLLVG DAELAKQASD KLLEEHGIYV QAINYPTVPR GEERLRITPT
     PGHTQELRDH LVEAVNTVWN DLGIKRASDW KAMGGFVGVG VEAAELENQP IWTDAQLNMR
     PDETLEAAVE REFQAAVPGM KAGGAKAKPV GSIAANPIGA SIPVAAAA
//