ID   HEM1_CHICK              Reviewed;         635 AA.
AC   P07997;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 2.
DT   16-JUN-2009, entry version 77.
DE   RecName: Full=5-aminolevulinate synthase, nonspecific, 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-H;
DE   Flags: Precursor;
GN   Name=ALAS1; Synonyms=ALASN;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC   Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   MEDLINE=86148479; PubMed=3005973; DOI=10.1093/nar/14.3.1379;
RA   Maguire D.J., Day A.R., Borthwick I.A., Srivastava G., Wigley P.L.,
RA   May B.K., Elliott W.H.;
RT   "Nucleotide sequence of the chicken 5-aminolevulinate synthase gene.";
RL   Nucleic Acids Res. 14:1379-1391(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=85257679; PubMed=3839458;
RX   DOI=10.1111/j.1432-1033.1985.tb09047.x;
RA   Borthwick I.A., Srivastava G., Day A.R., Pirola B.A., Snoswell M.A.,
RA   May B.K., Elliott W.H.;
RT   "Complete nucleotide sequence of hepatic 5-aminolaevulinate synthase
RT   precursor.";
RL   Eur. J. Biochem. 150:481-484(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=89128863; PubMed=2915978; DOI=10.1073/pnas.86.3.792;
RA   Riddle R.D., Yamamoto M., Engel J.D.;
RT   "Expression of delta-aminolevulinate synthase in avian cells: separate
RT   genes encode erythroid-specific and nonspecific isozymes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:792-796(1989).
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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; X02827; CAA26595.1; -; mRNA.
DR   EMBL; X03517; CAA27223.1; -; Genomic_DNA.
DR   EMBL; X03627; CAA27223.1; JOINED; Genomic_DNA.
DR   IPI; IPI00584086; -.
DR   PIR; A23538; SYCHAL.
DR   RefSeq; NP_001018012.1; -.
DR   UniGene; Gga.1399; -.
DR   HSSP; P12998; 1BS0.
DR   GeneID; 552895; -.
DR   KEGG; gga:552895; -.
DR   HOVERGEN; P07997; -.
DR   BRENDA; 2.3.1.37; 4.
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     56       Mitochondrion.
FT   CHAIN        57    635       5-aminolevulinate synthase, nonspecific,
FT                                mitochondrial.
FT                                /FTId=PRO_0000001233.
FT   MOD_RES     440    440       N6-(pyridoxal phosphate)lysine
FT                                (Probable).
FT   CONFLICT     53     53       S -> A (in Ref. 2 and 3).
SQ   SEQUENCE   635 AA;  69948 MW;  EEE708B85C1539BA CRC64;
     MEAVVRRCPF LARVSQAFLQ KAGPSLLFYA QHCPKMMEAA PPAAARGLAT SASRGQQVEE
     TPAAQPEAKK AKEVAQQNTD GSQPPAGHPP AAAVQSSATK CPFLAAQMNH KSSNVFCKAS
     LELQEDVKEM QVDRKGKEFA KIPTNSVVRN TEAEGEEQSG LLKKFKDIML KQRPESVSHL
     LQDNLPKSVS TFQYDQFFEK KIDEKKKDHT YRVFKTVNRK AQIFPMADDY SDSLITKKEV
     SVWCSNDYLG MSRHPRVCGA VMDTLKQHGA GAGGTRNISG TSKFHVDLEK ELADLHGKDA
     ALLFSSCFVA NDSTLFTLAK MLPGCEIYSD SGNHASMIQG IRNSRVPKHI FRHNDVNHLR
     ELLKKSDPST PKIVAFETVH SMDGAVCPLE ELCDVAHEHG AITFVDEVHA VGLYGARGGG
     IGDRDGVMHK MDIISGTLGK AFACVGGYIS STSALIDTVR SYAAGFIFTT SLPPMLLAGA
     LESVRTLKSA EGQVLRRQHQ RNVKLMRQML MDAGLPVVHC PSHIIPIRVA DAAKNTEICD
     KLMSQHSIYV QAINYPTVPR GEELLRIAPT PHHTPQMMSY FLEKLLATWK DVGLELKPHS
     SAECNFCRRP LHFEVMSERE RSYFSGMSKL LSVSA
//