ID A0A1V6SFB0_9EURO Unreviewed; 644 AA.
AC A0A1V6SFB0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-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 ORFNames=PENVUL_c001G08978 {ECO:0000313|EMBL:OQE12608.1};
OS Penicillium vulpinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE12608.1, ECO:0000313|Proteomes:UP000191518};
RN [1] {ECO:0000313|Proteomes:UP000191518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- FUNCTION: Catalyzes the synthesis of 5-aminolevulinate (ALA) from
CC succinyl-CoA and glycine, the first and rate-limiting step in heme
CC biosynthesis. {ECO:0000256|ARBA:ARBA00003076}.
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:ARBA00001588,
CC 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: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 matrix
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:RU003693}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQE12608.1}.
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DR EMBL; MDYP01000001; OQE12608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6SFB0; -.
DR STRING; 29845.A0A1V6SFB0; -.
DR OrthoDB; 9643at2759; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000191518; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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; 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: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 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 Mitochondrion {ECO:0000256|RuleBase:RU910713};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693};
KW Reference proteome {ECO:0000313|Proteomes:UP000191518};
KW Transferase {ECO:0000256|RuleBase:RU910713}.
FT DOMAIN 192..552
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 90..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 644 AA; 69123 MW; 9DF7427729C7D9FD CRC64;
MEALLQQSRT MCPFLKRTSP TTLRTLSTAT RPSTSPGGGT MSNLQVLGRR CPVMSKALAV
QSARLSGTKR FASRAAGVTG IQHMRFPTGK RELHTTGGHP ASLASGGYEK NERGNPNLAN
PLRPSPATGH AGAAVRGPRP EAPTTKKFNY DDFYNVELEK KHKDKSYRYF NNINRLAKEF
PRAHTASAEE RVTVWCSNDY LGMGRNPQVL DSMHKTLDTY GAGAGGTRNI SGHNQHAIAL
EDTLAKLHGK EAALVFSSCF VANDATLATL GSKMPDCVIL SDSLNHASMI QGIRHSGAKK
MVFKHNDMED LEAKLASLPL GTPKIIAFES VYSMCGSIAP IEKICDLSDK YGAITFLDEV
HAVGMYGPHG AGVAEHLDFD VYASQDTAFP QSTKGTVQDR IDIITGTLGK AYGCVGGYIA
GSAAMVDTIR SLAPGFIFTT SLPPATMAGA DAAIQYQSQQ PRDRVLQQLH TRAVKTALND
LDIPVIPNPS HIVPLLVGDA ELAKKASDKL LEEHGIYVQA INYPTVPRGE ERLRITPTPG
HVKHLREHLV QAVQAVWNDL GLKRTSDWKS QGGFVGVGVE GAEAANQPIW EDTQLGLQVN
ETLEGAVARE FNDAAVQAAV PLKAATPLTE KAYSGMNSTA GVVA
//
