ID A0A668RN46_OREAU Unreviewed; 615 AA.
AC A0A668RN46;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 18-JUN-2025, entry version 24.
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=ALAS1 {ECO:0000313|Ensembl:ENSOABP00000005802.1};
OS Oreochromis aureus (Israeli tilapia) (Chromis aureus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=47969 {ECO:0000313|Ensembl:ENSOABP00000005802.1, ECO:0000313|Proteomes:UP000472276};
RN [1] {ECO:0000313|Ensembl:ENSOABP00000005802.1}
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.
CC {ECO:0000256|ARBA:ARBA00037218}.
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 -!- 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; A0A668RN46; -.
DR Ensembl; ENSOABT00000006014.2; ENSOABP00000005802.1; ENSOABG00000003232.2.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000472276; Unassembled WGS sequence.
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; 3.40.640.10:FF:000006; 5-aminolevulinate synthase, mitochondrial; 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:SF50; 5-AMINOLEVULINATE SYNTHASE, NON-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};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW 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:UP000472276};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU910713};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 3..125
FT /note="5-aminolevulinate synthase presequence"
FT /evidence="ECO:0000259|Pfam:PF09029"
FT DOMAIN 224..565
FT /note="Aminotransferase class I/classII large"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 51..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 68289 MW; C2C76C53D77EC1DF CRC64;
MDVIVRRCPF LARMPQAFLQ QSKKALVTYA QRCPIMMELA AKPMAPSMAR ALCSSSSSHQ
KPENTVSAGE DDKDESKLPA GHPMPPPGQM MASKCPFLAA EMSQKNSGVV RQVGIEFQED
VQEVRTVKKE VTADQLKQPN LASTTEGETT LMRTLLKQRP KKVSHLLQDN LPGRSTFYYD
AFFEKKIEEK KNDHTYRVFK TVNRRATEFP MADDFTSSLQ EKRDVSVWCS NDYLGMSRHP
RVVQSIMDTL QKHGSGAGGT RNISGTSKFH VELEQELADL HKKDAALLFT SCFVANDSTL
FTLAKMLPGC EIYSDAGNHA SMIQGIRNSG AKKFIFRHND VAHLRELLEK GDPTKPKIVA
FETVHSMDGL CAFLSVTGFG AITFVDEVHA VGLYGSRGGG IGDRDGVMHK MDIISGTLGK
AFGCVGGYIA STAALVDTVR SYAAGFIFTT SLPPMLLAGA RQSIQVLKGE EGRSLRRKHQ
RNVKLLRQML MDSGLPVVHC PSHIIPVRVS NAEKNTEVCD IMMRRHNIYV QAINYPTVAR
GDELLRIAPT PHHTPEMMKY FVGKLEQTWK EVGLELKPHS SAECTFCQQP LHFEVMSERE
KSYFNGLSHL ISACA
//
