ID   HEM0_BOVIN              Reviewed;         587 AA.
AC   Q3ZC31;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=5-aminolevulinate synthase, erythroid-specific, 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            Short=ALAS-E;
DE   Flags: Precursor;
GN   Name=ALAS2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- MISCELLANEOUS: There are two delta-ALA synthetase in vertebrates:
CC       an erythroid- specific form and one (housekeeping) which is
CC       expressed in all tissues.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family.
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DR   EMBL; BC102938; AAI02939.1; -; mRNA.
DR   IPI; IPI00707059; -.
DR   RefSeq; NP_001030275.1; -.
DR   UniGene; Bt.49467; -.
DR   SMR; Q3ZC31; 1-49.
DR   Ensembl; ENSBTAG00000013178; Bos taurus.
DR   GeneID; 511791; -.
DR   KEGG; bta:511791; -.
DR   HOVERGEN; Q3ZC31; -.
DR   OMA; Q3ZC31; DVSMAAC.
DR   BRENDA; 2.3.1.37; 251.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0003870; F:5-aminolevulinate synthase activity; ISS:UniProtKB.
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   GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR   InterPro; IPR010961; 4pyrrol_synth_NH2levulA_synth.
DR   InterPro; IPR015118; 5aminolev_synth_preseq.
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   Pfam; PF09029; Preseq_ALAS; 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    ?49       Mitochondrion (Potential).
FT   CHAIN       ?50    587       5-aminolevulinate synthase, erythroid-
FT                                specific, mitochondrial.
FT                                /FTId=PRO_0000280705.
FT   MOD_RES     391    391       N6-(pyridoxal phosphate)lysine
FT                                (Probable).
SQ   SEQUENCE   587 AA;  65137 MW;  8D0D94383137F5DC CRC64;
     MVTAAMLLQR CPVLIRSPTG LLGKMIKTHQ FLFGIGRCPI LATQGPSFSQ IHLKATKAGG
     DSPSWAKSHC PFMLLELQDG KSKIVQKAAP EVQEDVKTFK TDLPTSLAST SLKKTFSSPQ
     EPEKNSEKVT HLIQNNMAGD HVFGYDQFFR DKIMEKKQDH TYRVFKTVNR WADAYPFAEH
     FFEASVASKD VSVWCSNDYL GMSRHPRVLQ ATQEILQRHG AGAGGTRNIS GTSKFHVELE
     QELAELHQKD SALLFSSCFV ANDSTLFTLA KILPGCEIYS DAGNHASMIQ GIRNSGAAKF
     VFRHNDPDHL KKLLKKSNPE TPKIVAFETV HSMDGAICPL EELCDVAHQY GALTFVDEVH
     AVGLYGSRGA GIGERDGIMH KIDIISGTLG KAFGCVGGYI ASTRDLVDMV RSYAAGFIFT
     TSLPPMVLSG ALESVRLLKG EEGQALRRAH QRNVKHMRQL LMDRGLPVIP CPSHIIPIRV
     GDAMLNTRIC DLLLSKYGIY VQAINYPTVP RGEELLRLAP SPHHSPQMME DFVEKLLEAW
     TEVGLPLQDI SIAACNFCRR PVHFELMSEW ERSYFGNMGP QYVTTYA
//