ID   HEM1_CANAL              Reviewed;         564 AA.
AC   O94069; A0A1D8PS41; Q5A965;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   27-MAR-2024, entry version 142.
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=CAALFM_CR02000CA;
GN   ORFNames=Ca49C4.15, CaO19.2601;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1161;
RA   Murphy L., Harris D., Barrell B.G., Rajandream M.A.;
RT   "Candida albicans strain 1161 genome pilot sequencing project.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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}.
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DR   EMBL; AL033503; CAA22025.1; -; Genomic_DNA.
DR   EMBL; CP017630; AOW30952.1; -; Genomic_DNA.
DR   PIR; T18251; T18251.
DR   RefSeq; XP_718266.2; XM_713173.2.
DR   AlphaFoldDB; O94069; -.
DR   SMR; O94069; -.
DR   STRING; 237561.O94069; -.
DR   EnsemblFungi; CR_02000C_A-T; CR_02000C_A-T-p1; CR_02000C_A.
DR   GeneID; 3640149; -.
DR   KEGG; cal:CAALFM_CR02000CA; -.
DR   CGD; CAL0000189686; HEM1.
DR   VEuPathDB; FungiDB:CR_02000C_A; -.
DR   eggNOG; KOG1360; Eukaryota.
DR   HOGENOM; CLU_015846_6_0_1; -.
DR   InParanoid; O94069; -.
DR   OMA; ARRCPIM; -.
DR   OrthoDB; 9643at2759; -.
DR   UniPathway; UPA00251; UER00375.
DR   Proteomes; UP000000559; Chromosome R.
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; IMP:CGD.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006783; P:heme biosynthetic process; IMP:CGD.
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..57
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           58..564
FT                   /note="5-aminolevulinate synthase, mitochondrial"
FT                   /id="PRO_0000001237"
FT   ACT_SITE        353
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         278
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         306
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         350
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         382
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         383
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         468
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   MOD_RES         353
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   CONFLICT        64
FT                   /note="A -> V (in Ref. 1; CAA22025)"
FT   CONFLICT        81
FT                   /note="T -> S (in Ref. 1; CAA22025)"
SQ   SEQUENCE   564 AA;  61381 MW;  4282832A9F27AF2D CRC64;
     MESITKVSMS VCPFVRSTST QALRQLSQTS GALANQARQC PIAGNAIRAK EISIRSYSSA
     TKPARATAAT PSTPEATFNV TSSFELGSKE TAFDYNGYLG NELEKKRSDK SYRYFNNINR
     LANEFPKAHR TQEEDKVTVW CSNDYLGMGK NENTLKEMKR VLDKYGSGAG GTRNIAGHNS
     HAIKLESELA ALHKHDAALV FSSCFVANDA VLSLLGQKIK DLVIFSDELN HASMIQGIRN
     SRARKHIFKH NNLADLESKL AQYPKSTPKL IAFESVYSMC GSIAPIEAIC DLAEKYGALT
     FLDEVHAVGM YGPHGAGVAE HLNFEAHLKS GIERPEITTV MSRVDMVTGT LGKAYGVVGG
     YITGKTNLID WFRSYAPGFI FTTSLPPAIM AGCSASIRYQ RATLKDRIAQ QKNTRLVKNN
     LNELGIPVIP NPSHIVPVLV GNAADAKRAS DLLLNKHDIY VQAINFPTVP IGEERLRITP
     TPGHGPELSK QLVEAVDSVF TELNLNRIND WKKLGGLVGV GVEGAAKVEH IWTEEQLALT
     DADLNPNVVN PAISPLDVSS GIST
//