HEM1_YARLI
ID HEM1_YARLI Reviewed; 563 AA.
AC Q6CCW0;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=YALI0C06083g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
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DR EMBL; CR382129; CAG81803.1; -; Genomic_DNA.
DR RefSeq; XP_501502.1; XM_501502.1.
DR AlphaFoldDB; Q6CCW0; -.
DR SMR; Q6CCW0; -.
DR STRING; 4952.CAG81803; -.
DR EnsemblFungi; CAG81803; CAG81803; YALI0_C06083g.
DR GeneID; 2909236; -.
DR KEGG; yli:YALI0C06083g; -.
DR VEuPathDB; FungiDB:YALI0_C06083g; -.
DR HOGENOM; CLU_015846_6_0_1; -.
DR InParanoid; Q6CCW0; -.
DR OMA; NHASMIV; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000001300; Chromosome C.
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 Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01821; 5aminolev_synth; 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..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 19..563
FT /note="5-aminolevulinate synthase, mitochondrial"
FT /id="PRO_0000001244"
FT ACT_SITE 376
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 303
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 331
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 373
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 405
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 406
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 491
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT MOD_RES 376
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P18079"
SQ SEQUENCE 563 AA; 61237 MW; FC7BBC2F382C0170 CRC64;
MESLVRQSKK LCPYIGRTSA SSLKQLGNGR LTQKAGQCPI MGKAMGVRGF KSDAGSNAES
ATVDVHAAVD TSKGTCPHAA QYSPVYPSSR LDNYPFGMTQ RGLGKVPTQD AHNATTFNYE
SFYENKINAK HQDKSYRYFN NINRLAAEFP RAHRGSIEED KVTVWCANDY LGMGRNPVVV
DAMHETLDKY GAGAGGTRNI AGHNRHAVEL EAAIADLHKK EAALVFSSCY VANDSTLSLL
GQALPNCVYF SDASNHASMI HGIRHGGSEK VVWKHNDLAD LEAKLARYPK STPKVIAFES
VYSMCGSIGP IEEICDLADK YGAITFLDEV HAVGMYGPTG AGVAEHLDFE HYHSGAQTQR
QPIMDRVDIF TGTLGKAYGC VGGYIAGSAK FVDMVRSYAP GFIFTTTLPP ATMAGARAAI
NYQKATMKDR VAQQTHTRYV KDKLANRGIP VVPNPSHIVP VLVGDAQKAK AASDLLLTKH
QIYVQAINFP TVPIGQERLR VTPTPGHHEG LCDELVAALE DVWQELDLKR VEDWTAEGGL
CGVGEGVEVE PLWSEEQLSY GRD
