ID A0A5F4WLR3_CALJA Unreviewed; 570 AA.
AC A0A5F4WLR3;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 18-JUN-2025, entry version 25.
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:ENSCJAP00000078555.2};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000078555.2, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000078555.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000078555.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) 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 AlphaFoldDB; A0A5F4WLR3; -.
DR Ensembl; ENSCJAT00000089438.2; ENSCJAP00000078555.2; ENSCJAG00000016542.5.
DR GeneTree; ENSGT00940000159912; -.
DR OMA; DQFFRNK; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000008225; Chromosome X.
DR Bgee; ENSCJAG00000016542; Expressed in heart and 6 other cell types or tissues.
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:0048821; P:erythrocyte development; IEA:TreeGrafter.
DR GO; GO:0042541; P:hemoglobin biosynthetic process; IEA:TreeGrafter.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU910713};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..570
FT /note="5-aminolevulinate synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035187801"
FT DOMAIN 7..97
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 570 AA; 62519 MW; 6838B02AF856B511 CRC64;
MVTAAMLLQC CPVLARGPTS LLGKVVKAHQ FLFGIGRCPI LATQGPNCSQ IHLKATKAGG
DSPSWAKGHC PFMLSELQDG KSKIVQKAAP EVQEDVKVFK TDLPSSLVSA SLRKPFSGPQ
EQEQIYGKVT HLIQNNMPGN YVFSYDQFFR DKITEKKQDH TYRVFKTVNR WADAYPFAQH
FSEASVASKD VSVWCSNDYL GMSRHPQVLQ ATQETLQRHG AGAGGTRNIS GTSKFHVELE
QELAELHQKD SALLFSSCFV ANDSTLFTLA KILPGCEIYS DAGNHASMIQ GIRNSGAAKF
VFRHNDPDHL KKLLEKSNPE TPKIVAFETV HSMDGAICPL EELCDVSHQY GALTFVDEVH
AVGLYGSRGA GIGERDGIMH KIDIISGTLG KAFGCVGGYI ASTRDLVDMV RSYAAGFIFT
TSLPPMVLSG ALESVRLLKG EEGQALRRAH QRNVKHMRQL LMDRGLPVIP CPSHIIPIRV
GDAALNSKLC DLLLSKHGIY VQAINYPTVP RGEELLRLAP SPHHSPQMME DFVEKLLLAW
TEVGPPMLNS FIWADTCTGD FSAPVLPSLR
//
