ID A0A1S3IGI8_LINUN Unreviewed; 576 AA.
AC A0A1S3IGI8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=LOC106164039 {ECO:0000313|RefSeq:XP_013397253.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013397253.1};
RN [1] {ECO:0000313|RefSeq:XP_013397253.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013397253.1};
RG RefSeq;
RL Submitted (NOV-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|RuleBase:RU910713};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU910713};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from glycine: step 1/1.
CC {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:RU910713}.
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DR RefSeq; XP_013397253.1; XM_013541799.1.
DR AlphaFoldDB; A0A1S3IGI8; -.
DR EnsemblMetazoa; XM_013541799.1; XP_013397253.1; LOC106164039.
DR GeneID; 106164039; -.
DR OrthoDB; 9643at2759; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:InterPro.
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: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; 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:SF105; 5-AMINOLEVULINATE SYNTHASE; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU910713};
KW Heme biosynthesis {ECO:0000256|RuleBase:RU910713};
KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU910713};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Transferase {ECO:0000256|RuleBase:RU910713}.
FT DOMAIN 5..74
FT /note="5-aminolevulinate synthase presequence"
FT /evidence="ECO:0000259|Pfam:PF09029"
FT DOMAIN 176..522
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 101..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 576 AA; 63453 MW; 4735E5EF48E8174C CRC64;
MKALKCPFLT RIPTNHLRQY APAVLSYAEN CPIMGHVIKF ASMATRAGTP PSEPTNLNKC
PYLSSEAKRK QSTSAAAAIT QGSVESAAKV DIATKVTSQS LDNQAGQKKE ETLNVNSTSA
SRGGHAEPFK YFNYEQFFQN EIEKKKTDHS YRVFRKVNRR AEKFPFAEEH TEGKKDITVW
CSNDYLGMSW HPKVKQAVVN AVREHGAGAG GTRNISGNTI YHEELEAELA DLHQKEGALL
FTSCYVANDS TLFTLAKALP GCHIFSDAGN HASMIQGIRN SGVPKHIFRH NDPVHLEELL
KKVDVNTPKI VAFETVHSMT GAVCPLEELC DVAHKYGAIT FVDEVHAVGL YGDRGAGVGE
RDQLLHKMDI ISGTLGKAFG NIGGYIASSS RLVDMIRSYA SGFIFTTSLP PTVLSGALAS
IRVLKSDEGR KLRQTHQENV RHLRKKLTEA GLPVIHCPSH IIPIHVGDAQ AVTQVANTLL
KKHKIYVQGI NYPTVPRGEE KLRIAPTPHH TEDMMEYFVK AVVDAWEESG MEFTSSPCPS
TCEFCNRPGD FAAKEARHCT RPDCQWEEAQ ETVTAA
//
