ID   A2AFM0_MOUSE            Unreviewed;       587 AA.
AC   A2AFM0;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   02-SEP-2026, entry version 144.
DE   RecName: Full=5-aminolevulinate synthase {ECO:0000256|RuleBase:RU910713};
DE            EC=2.3.1.37 {ECO:0000256|RuleBase:RU910713};
DE   AltName: Full=5-aminolevulinic acid synthase {ECO:0000256|RuleBase:RU910713};
DE   AltName: Full=Delta-ALA synthase {ECO:0000256|RuleBase:RU910713};
DE   AltName: Full=Delta-aminolevulinate synthase {ECO:0000256|RuleBase:RU910713};
GN   Name=Alas2 {ECO:0000313|EMBL:AAI50871.1, ECO:0000313|MGI:MGI:87990};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:AAI50871.1};
RN   [1] {ECO:0000313|EMBL:AAI50871.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000313|EMBL:AAI50871.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent
CC       condensation of succinyl-CoA and glycine to form aminolevulinic acid
CC       (ALA), with CoA and CO2 as by-products. Contributes significantly to
CC       heme formation during erythropoiesis. {ECO:0000256|ARBA:ARBA00045913}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=succinyl-CoA + glycine + H(+) = 5-aminolevulinate + CO2 + CoA;
CC         Xref=Rhea:RHEA:12921, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:356416; EC=2.3.1.37;
CC         Evidence={ECO:0000256|ARBA:ARBA00049013};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12922;
CC         Evidence={ECO:0000256|ARBA:ARBA00049013};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU003693};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from glycine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005029, ECO:0000256|RuleBase:RU910713}.
CC   -!- SUBUNIT: Homodimer. Interacts with SUCLA2.
CC       {ECO:0000256|ARBA:ARBA00065724}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|RuleBase:RU910713}; Peripheral membrane protein
CC       {ECO:0000256|RuleBase:RU910713}. Note=Localizes to the matrix side of
CC       the mitochondrion inner membrane. {ECO:0000256|RuleBase:RU910713}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008392,
CC       ECO:0000256|RuleBase:RU003693}.
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DR   EMBL; BC150870; AAI50871.1; -; mRNA.
DR   RefSeq; NP_033783.1; NM_009653.4.
DR   AlphaFoldDB; A2AFM0; -.
DR   SMR; A2AFM0; -.
DR   Antibodypedia; 457; 319 antibodies from 34 providers.
DR   DNASU; 11656; -.
DR   GeneID; 11656; -.
DR   KEGG; mmu:11656; -.
DR   AGR; MGI:87990; -.
DR   CTD; 212; -.
DR   MGI; MGI:87990; Alas2.
DR   VEuPathDB; HostDB:ENSMUSG00000025270; -.
DR   OMA; DQFFRNK; -.
DR   OrthoDB; 10263824at2759; -.
DR   PhylomeDB; A2AFM0; -.
DR   UniPathway; UPA00251; UER00375.
DR   BioGRID-ORCS; 11656; 2 hits in 77 CRISPR screens.
DR   ExpressionAtlas; A2AFM0; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-UniRule.
DR   GO; GO:0003870; F:5-aminolevulinate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006785; P:heme B biosynthetic process; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   CDD; cd06454; KBL_like; 1.
DR   FunFam; 3.90.1150.10:FF:000029; 5-aminolevulinate synthase; 1.
DR   FunFam; 4.10.92.10:FF:000001; 5-aminolevulinate synthase; 1.
DR   FunFam; 3.40.640.10:FF:000006; 5-aminolevulinate synthase, mitochondrial; 1.
DR   Gene3D; 4.10.92.10; Aminolevulinic Acid Synthase 2; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010961; 4pyrrol_synth_NH2levulA_synth.
DR   InterPro; IPR015118; 5aminolev_synth_preseq.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II_large.
DR   InterPro; IPR050087; AON_synthase_class-II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01821; 5aminolev_synth; 1.
DR   PANTHER; PTHR13693:SF58; 5-AMINOLEVULINATE SYNTHASE, ERYTHROID-SPECIFIC, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   Pfam; PF09029; Preseq_ALAS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU910713};
KW   Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133,
KW   ECO:0000256|RuleBase:RU910713}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|RuleBase:RU910713};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003693};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU910713};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          6..99
FT                   /note="5-aminolevulinate synthase presequence"
FT                   /evidence="ECO:0000259|Pfam:PF09029"
FT   DOMAIN          190..536
FT                   /note="Aminotransferase class I/classII large"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   587 AA;  64753 MW;  A878D79FAD5B9856 CRC64;
     MVAAAMLLRS CPVLSQGPTG LLGKVAKTYQ FLFSIGRCPI LATQGPTCSQ IHLKATKAGG
     DSPSWAKSHC PFMLSELQDR KSKIVQRAAP EVQEDVKTFK TDLLSTMDST TRSHSFPSFQ
     EPEQTEGAVP HLIQNNMTGS QAFGYDQFFR DKIMEKKQDH TYRVFKTVNR WANAYPFAQH
     FSEASMASKD VSVWCSNDYL GISRHPRVLQ AIEETLKNHG AGAGGTRNIS GTSKFHVELE
     QELAELHQKD SALLFSSCFV ANDSTLFTLA KLLPGCEIYS DAGNHASMIQ GIRNSGAAKF
     VFRHNDPGHL KKLLEKSDPK TPKIVAFETV HSMDGAICPL EELCDVAHQY GALTFVDEVH
     AVGLYGARGA GIGERDGIMH KLDIISGTLG KAFGCVGGYI ASTRDLVDMV RSYAAGFIFT
     TSLPPMVLSG ALESVRLLKG EEGQALRRAH QRNVKHMRQL LMDRGFPVIP CPSHIIPIRV
     GNAALNSKIC DLLLSKHSIY VQAINYPTVP RGEELLRLAP SPHHSPQMME NFVEKLLLAW
     TEVGLPLQDV SVAACNFCHR PVHFELMSEW ERSYFGNMGP QYVTTYA
//