ID   A2AFM1_MOUSE            Unreviewed;       572 AA.
AC   A2AFM1;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   02-SEP-2026, entry version 142.
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|Ensembl:ENSMUSP00000108335.2,
GN   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|Ensembl:ENSMUSP00000108335.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000108335.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000108335.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RG   Mouse Genome Sequencing Consortium;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
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).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000108335.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000108335.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=21750661;
RA   Church D.M., Schneider V.A., Graves T., Auger K., Cunningham F., Bouk N.,
RA   Chen H.C., Agarwala R., McLaren W.M., Ritchie G.R., Albracht D.,
RA   Kremitzki M., Rock S., Kotkiewicz H., Kremitzki C., Wollam A., Trani L.,
RA   Fulton L., Fulton R., Matthews L., Whitehead S., Chow W., Torrance J.,
RA   Dunn M., Harden G., Threadgold G., Wood J., Collins J., Heath P.,
RA   Griffiths G., Pelan S., Grafham D., Eichler E.E., Weinstock G.,
RA   Mardis E.R., Wilson R.K., Howe K., Flicek P., Hubbard T.;
RT   "Modernizing reference genome assemblies.";
RL   PLoS Biol. 9:e1001091-e1001091(2011).
RN   [4] {ECO:0000313|Ensembl:ENSMUSP00000108335.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000108335.2};
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
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   RefSeq; NP_001095916.1; NM_001102446.2.
DR   AlphaFoldDB; A2AFM1; -.
DR   SMR; A2AFM1; -.
DR   ProteomicsDB; 320150; -.
DR   Antibodypedia; 457; 319 antibodies from 34 providers.
DR   DNASU; 11656; -.
DR   Ensembl; ENSMUST00000112715.2; ENSMUSP00000108335.2; ENSMUSG00000025270.14.
DR   GeneID; 11656; -.
DR   UCSC; uc009uok.1; mouse.
DR   AGR; MGI:87990; -.
DR   CTD; 212; -.
DR   MGI; MGI:87990; Alas2.
DR   VEuPathDB; HostDB:ENSMUSG00000025270; -.
DR   GeneTree; ENSGT00940000159912; -.
DR   HOGENOM; CLU_015846_6_1_1; -.
DR   OrthoDB; 10263824at2759; -.
DR   UniPathway; UPA00251; UER00375.
DR   BioGRID-ORCS; 11656; 2 hits in 77 CRISPR screens.
DR   Proteomes; UP000000589; Chromosome X.
DR   Bgee; ENSMUSG00000025270; Expressed in blood and 172 other cell types or tissues.
DR   ExpressionAtlas; A2AFM1; 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:0033014; P:tetrapyrrole biosynthetic process; IEA:InterPro.
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; 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   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   Proteomics identification {ECO:0007829|ProteomicsDB:A2AFM1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003693};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU910713};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          175..521
FT                   /note="Aminotransferase class I/classII large"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   572 AA;  63078 MW;  F4B49A3A2F39F989 CRC64;
     MVAAAMLLRS CPVLSQGPTG LLGKVAKTYQ FLFSIGRCPI LATQGPTCSQ IHLKATKAGG
     ELQDRKSKIV QRAAPEVQED VKTFKTDLLS TMDSTTRSHS FPSFQEPEQT EGAVPHLIQN
     NMTGSQAFGY DQFFRDKIME KKQDHTYRVF KTVNRWANAY PFAQHFSEAS MASKDVSVWC
     SNDYLGISRH PRVLQAIEET LKNHGAGAGG TRNISGTSKF HVELEQELAE LHQKDSALLF
     SSCFVANDST LFTLAKLLPG CEIYSDAGNH ASMIQGIRNS GAAKFVFRHN DPGHLKKLLE
     KSDPKTPKIV AFETVHSMDG AICPLEELCD VAHQYGALTF VDEVHAVGLY GARGAGIGER
     DGIMHKLDII SGTLGKAFGC VGGYIASTRD LVDMVRSYAA GFIFTTSLPP MVLSGALESV
     RLLKGEEGQA LRRAHQRNVK HMRQLLMDRG FPVIPCPSHI IPIRVGNAAL NSKICDLLLS
     KHSIYVQAIN YPTVPRGEEL LRLAPSPHHS PQMMENFVEK LLLAWTEVGL PLQDVSVAAC
     NFCHRPVHFE LMSEWERSYF GNMGPQYVTT YA
//