ID A0A3B3D2Q3_ORYME Unreviewed; 591 AA.
AC A0A3B3D2Q3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
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};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000023704.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000023704.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + H(+) + succinyl-CoA = 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:ARBA00033616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12922;
CC Evidence={ECO:0000256|ARBA:ARBA00033616};
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; A0A3B3D2Q3; -.
DR STRING; 30732.ENSOMEP00000023704; -.
DR PaxDb; 30732-ENSOMEP00000023704; -.
DR Ensembl; ENSOMET00000011526.1; ENSOMEP00000023704.1; ENSOMEG00000000855.1.
DR GeneTree; ENSGT00940000159912; -.
DR OMA; ARRCPIM; -.
DR OrthoDB; 9643at2759; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000261560; Unplaced.
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:0035162; P:embryonic hemopoiesis; IEA:Ensembl.
DR GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
DR GO; GO:0042541; P:hemoglobin biosynthetic process; IEA:Ensembl.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06454; KBL_like; 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.
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693};
KW Transferase {ECO:0000256|RuleBase:RU910713}.
FT DOMAIN 3..110
FT /note="5-aminolevulinate synthase presequence"
FT /evidence="ECO:0000259|Pfam:PF09029"
FT DOMAIN 197..540
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 46..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 591 AA; 64956 MW; C1133ECE393DF12B CRC64;
MAAFLHHCPF LKSAPKPALR RTGASLLSLA EKCPIITRQI TVSGPASLDS KLSSPTTTSK
HKQLSTVEQK RQFAQTATHV AASMSKACPF VSSQIGVVQA SPEVQEDVQD GLMKSLLKGL
KDSMFPSGSD LNSITHLLRD NMVGPSYDYD HFFTEKISEK KKDHTYRVFK TVNRSAKTFP
FAEDYSIPGR AGAQVSVWCS NDYLGMSRHP KVLGAIREAL EKYGAGAGGT RNISGTSNFH
VALERELAQL HRKDAALVFS SCFVANDSTL FTLAKMLPGC EIYSDAGNHA SMIQGIRNSG
AKRFIFRHND RRHLEELLQR SDPKTPKIVA FETVHSMDGA ICPLEELCDT AHRYGALTFV
DEVHAVGLYG AHGAGVGERD NIMHKIDIVS GTLGKAFGCV GGYVASSAAL VDTVRSYAAG
FIFTTALPPM VLAGALESVR VLRSAEGQVL RRAHQRNVKH MRQLLMDKGL PVVNCPSHII
PIRVGNAELN TKVCDILLEK YNIYVQAINY PTVPRGEELL RLAPSPHHEP DMMEYFVGKL
VEVWQEAGLP LNSPATAACT FCDRPLHFDL MSEWEKSYFG NMEPQYITVY A
//