ID A0A182M654_9DIPT Unreviewed; 602 AA.
AC A0A182M654;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 Anopheles culicifacies.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles; culicifacies species complex.
OX NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA010430-PA, ECO:0000313|Proteomes:UP000075883};
RN [1] {ECO:0000313|Proteomes:UP000075883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles culicifacies species A.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACUA010430-PA}
RP IDENTIFICATION.
RC STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA010430-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 EMBL; AXCM01002727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A182M654; -.
DR STRING; 139723.A0A182M654; -.
DR EnsemblMetazoa; ACUA010430-RA; ACUA010430-PA; ACUA010430.
DR VEuPathDB; VectorBase:ACUA010430; -.
DR OrthoDB; 9643at2759; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000075883; Unassembled WGS sequence.
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 Transferase {ECO:0000256|RuleBase:RU910713}.
FT DOMAIN 25..128
FT /note="5-aminolevulinate synthase presequence"
FT /evidence="ECO:0000259|Pfam:PF09029"
FT DOMAIN 195..538
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 69..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 66094 MW; A2F3EB6FB97BA4CD CRC64;
MIQLFNLTTS QFVARTVSSI KKMPCPFLTR LSTSYVRNYA PALLKAYGAQ CPVVQRTISS
LQGSQAGSGV AGGASAGTQD AAAKKETSAE ARRNLSSLQQ PKPVQSEQAA SSKQQQVGAK
KCPFLSTAAP HVKELGAESV EVPTERTFQY EDFFHEQILR KKQDHSYRVF KKVNRLAADG
QFPRALEYSW GERPITVWCS NDYLGMSCHP EVKRAVADAL ETYGTGAGGT RNISGNSMNH
ENLENRLAAL HQKESALLFT SCFVANDSTL FTLAKALPGC HIFSDAGNHA SMIQGIRNSG
VPKHIFRHND PAHLRELLQR VDRSLPKIVA FETVHSMTGA VCPLEELCDI AHEYGALTFV
DEVHAVGLYG EHGAGIGERE GQLHNMDIIS GTLGKAFGNV GGYIAGTALL VDMIRSYAAG
FIFTTSLPPT VLCGALKAVD ILASEEGRQL RARHQENVRY LRTRLQEEGF PVEHTPSHII
PVKIGNPRQC TEVSDQMIQR FGHYVQAINY PTVARGEEKL RLAPTPHHTY AMMDEMVRDM
KVVWQDLKMP LGGKHCPEEC AFCRKPLLFD RFEARTSASA ASCARELNCQ IPNCPQIAAV
AN
//
