ID HEM1_EREGS Reviewed; 556 AA. AC Q75DX7; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 107. DE RecName: Full=5-aminolevulinate synthase, mitochondrial; DE EC=2.3.1.37; DE AltName: Full=5-aminolevulinic acid synthase; DE AltName: Full=Delta-ALA synthase; DE AltName: Full=Delta-aminolevulinate synthase; DE Flags: Precursor; GN Name=HEM1; OrderedLocusNames=ABL104C; OS Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL OS Y-1056) (Yeast) (Ashbya gossypii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Eremothecium. OX NCBI_TaxID=284811; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056; RX PubMed=15001715; DOI=10.1126/science.1095781; RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., RA Gaffney T.D., Philippsen P.; RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces RT cerevisiae genome."; RL Science 304:304-307(2004). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056; RX PubMed=23749448; DOI=10.1534/g3.112.002881; RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.; RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type RT loci, numerous translocations, lack of transposons, and distinct gene RT duplications."; RL G3 (Bethesda) 3:1225-1239(2013). 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:0000250|UniProtKB:P09950}. 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:0000250|UniProtKB:P09950}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250|UniProtKB:P09950}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX CC biosynthesis; 5-aminolevulinate from glycine: step 1/1. CC {ECO:0000250|UniProtKB:P09950}. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P09950}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000250|UniProtKB:P09950}. CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE016815; AAS50667.1; -; Genomic_DNA. DR RefSeq; NP_982843.1; NM_208196.1. DR AlphaFoldDB; Q75DX7; -. DR SMR; Q75DX7; -. DR STRING; 284811.Q75DX7; -. DR EnsemblFungi; AAS50667; AAS50667; AGOS_ABL104C. DR GeneID; 4618923; -. DR KEGG; ago:AGOS_ABL104C; -. DR eggNOG; KOG1360; Eukaryota. DR HOGENOM; CLU_015846_6_0_1; -. DR InParanoid; Q75DX7; -. DR OMA; ARRCPIM; -. DR OrthoDB; 9643at2759; -. DR UniPathway; UPA00251; UER00375. DR Proteomes; UP000000591; Chromosome II. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0003870; F:5-aminolevulinate synthase activity; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central. DR GO; GO:1902117; P:positive regulation of organelle assembly; IEA:EnsemblFungi. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. 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; Heme biosynthesis; Mitochondrion; Pyridoxal phosphate; KW Reference proteome; Transferase; Transit peptide. FT TRANSIT 1..46 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 47..556 FT /note="5-aminolevulinate synthase, mitochondrial" FT /id="PRO_0000001236" FT ACT_SITE 345 FT /evidence="ECO:0000250|UniProtKB:P18079" FT BINDING 105 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P18079" FT BINDING 218 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P18079" FT BINDING 237 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P18079" FT BINDING 270 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P18079" FT BINDING 298 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P18079" FT BINDING 342 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P18079" FT BINDING 374 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P18079" FT BINDING 375 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P18079" FT BINDING 460 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P18079" FT MOD_RES 345 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000250|UniProtKB:P18079" SQ SEQUENCE 556 AA; 61222 MW; DABDD7E6FEB4E764 CRC64; MDSLARQSAK ICPFVSRVTS SMQQVQVLHK TNMSAMAQQC PVMRRAMAAR GYVTASPPAG AAAADVGEAR PITPVLERGT QERTFDYDGL FETELQKKRL DSSYRFFNNI NRLAKEYPMA HRLEEEDKVT VWCSNDYLTY SRNEKVMETM KRTIDKYGAG AGGTRNIAGH NRHAMRLEAE LAALHKKEGA LVFSSCFVAN DAVLSLLGQK MPNMVIFSDE MNHASMIMGI KHANVQKHIF RHNDLQHLEE LLAMYPKSQP KLIAFESVYS MSGSVADIRK ICDLAEKYGA LTFLDEVHSV GLYGPHGAGV AEHLDFEAHR KAGLASPAQT TVLDRVDMIT ATLGKSFGSV GGYLAASEKL VDFVRSYAPG FIFTSSLPPA VMAGSAAAVF DQRSSLHLRQ LQQKHTSYVK TGLGDLGIPV QPNPSHIVPV LVGNPDLAKR ASDILMEKHR IYVQAINFPT VPRGTERLRI TPTPGHTNDL SDVLLDAMDD VWKTLQLPRV SDWAAHGGLL GVGEPDYVPE ANLWTEEQMS LTNDDLHPSV FSPVEKFLEV SSGIKA //