HEM1_DEBHA
ID HEM1_DEBHA Reviewed; 575 AA.
AC Q6BX71;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=DEHA2B05478g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382134; CAG85193.1; -; Genomic_DNA.
DR RefSeq; XP_457198.1; XM_457198.1.
DR AlphaFoldDB; Q6BX71; -.
DR SMR; Q6BX71; -.
DR STRING; 4959.XP_457198.1; -.
DR PRIDE; Q6BX71; -.
DR EnsemblFungi; CAG85193; CAG85193; DEHA2B05478g.
DR GeneID; 2913002; -.
DR KEGG; dha:DEHA2B05478g; -.
DR VEuPathDB; FungiDB:DEHA2B05478g; -.
DR eggNOG; KOG1360; Eukaryota.
DR HOGENOM; CLU_015846_6_0_1; -.
DR InParanoid; Q6BX71; -.
DR OMA; NHASMIV; -.
DR OrthoDB; 930001at2759; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000000599; Chromosome B.
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:InterPro.
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..55
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 56..575
FT /note="5-aminolevulinate synthase, mitochondrial"
FT /id="PRO_0000001239"
FT ACT_SITE 364
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 289
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 317
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 361
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 393
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 394
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 479
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT MOD_RES 364
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P18079"
SQ SEQUENCE 575 AA; 62652 MW; 05107F73EB488A2C CRC64;
MESITRVSMS VCPFVKSSSA QALRQLSKNS ALTSQARQCP FMGAALNAKE STRSYSSATK
PVRATASSLA SNPPSTMQSK YSFKAEELVG NKDAINLESK ENTFDFKGYL NSELSKKRTD
KSYRFFNNIN RLANEFPKAH RSEENDKVTV WCSNDYLGMG KNENTINEMK RVLTKYGSGA
GGTRNIAGHN IHALKLESEL AALHKHEAAL VFSSCFVAND AVLSLFGQKI KDLVIFSDEL
NHASMIQGIR NSRAKKQVFK HNDLADLEEK LAQYPKSTPK LIAFESVYSM CGSIAPIEAI
CDLAEKYGAL TFLDEVHAVG MYGPHGAGVA EHLDFDAHLK SGIASPQTQT VMNRVDMVTG
TLGKAYGTVG GYITGKANLI DWFRSFAPGF IFTTTLPPSI MAGSSASIRY QRSTLQDRIA
QQTNTRYVKN NLTDIGIPVI PNPSHIVPVL VGNALDAKKA SDLLLDKYNI YVQAINFPTV
PIGQERLRIT PTPGHGPELS NQLIGALDSV FNELSLSRIG DWEGKGGLCG VGEPDIEPIE
HIWTSEQLAL TDADINPNVI DPVIQPIGVS SGVRD
