ID A0A3Q4GGV4_NEOBR Unreviewed; 613 AA.
AC A0A3Q4GGV4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, 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};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000005888.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000005888.1}
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; A0A3Q4GGV4; -.
DR STRING; 32507.ENSNBRP00000005888; -.
DR Ensembl; ENSNBRT00000006069.1; ENSNBRP00000005888.1; ENSNBRG00000004620.1.
DR GeneTree; ENSGT00940000159912; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000004620; Expressed in blood and 7 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: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; 2.
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|RuleBase:RU910713};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693};
KW Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW Transferase {ECO:0000256|RuleBase:RU910713}.
FT DOMAIN 42..87
FT /note="5-aminolevulinate synthase presequence"
FT /evidence="ECO:0000259|Pfam:PF09029"
FT DOMAIN 81..117
FT /note="5-aminolevulinate synthase presequence"
FT /evidence="ECO:0000259|Pfam:PF09029"
FT DOMAIN 219..562
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 613 AA; 67267 MW; D6742F4CCD334FCB CRC64;
TESPFGSSHS TTLCYVIYNL HPRKAKSSVL TQSKNSFSIM AAFLHHCPFL KLAPKPALRR
TGAALLSLAN HCPLIAPKLF AQTATQVAVS VSKGCPFVSS QIGMVRASPE VQEDVQERDK
VFINLTQSHS SLTDLMASLK GVKDSACPTS AQPNTVTHLL KDNMAGPSYD YDQFFMEKIA
VKKKDHSYRV FKTVNRSAEV FPFAEDYSIS GREGSQVSVW CSNDYLGMSR HPRVLSAIRD
ALDKHGAGAG GTRNISGTSN FHVSLEKELA ELHQKDAALV FSSCFVANDS TLFTLAKMLP
GCEIYSDAGN HASMIQGIRN SGAKRFIFRH NDGRHLEELL QRSDPTTPKI VAFETVHSMD
GAICPLEELC DVAHRYGALT FVDEVHAVGL YGAHGAGVGE RDNIMHKIDI VSGTLGKAFG
CVGGYIASSA ALVDTVRSYA AGFIFTTALP PMVLVGALES VRVLKSEEGQ ALRRAHQRNV
KHMRQLLMDK GLPVVNCPSH IIPIRVGNAE LNTKVCDILL ERHNIYVQAI NYPTVPRGEE
LLRLAPSPHH NPKMMEYFVG KLVDVWKEAG LLLNGPATAS CTFCDRPLHF DLMSEWEKSY
FGNMEPQYIT VYA
//
