HEM1_KLULA
ID HEM1_KLULA Reviewed; 570 AA.
AC P78698; Q6CT64;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 132.
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=KLLA0C15059g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=9271110;
RX DOI=10.1002/(sici)1097-0061(199708)13:10<961::aid-yea156>3.0.co;2-y;
RA Gonzales-Dominguez M., Mendez-Carro C., Cerdan M.E.;
RT "Isolation and characterization of the KlHEM1 gene in Kluyveromyces
RT lactis.";
RL Yeast 13:961-971(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; X92944; CAA63497.1; -; Genomic_DNA.
DR EMBL; CR382123; CAH01726.1; -; Genomic_DNA.
DR RefSeq; XP_452875.1; XM_452875.1.
DR AlphaFoldDB; P78698; -.
DR SMR; P78698; -.
DR STRING; 28985.XP_452875.1; -.
DR EnsemblFungi; CAH01726; CAH01726; KLLA0_C15059g.
DR GeneID; 2892616; -.
DR KEGG; kla:KLLA0_C15059g; -.
DR eggNOG; KOG1360; Eukaryota.
DR HOGENOM; CLU_015846_6_0_1; -.
DR InParanoid; P78698; -.
DR OMA; NHASMIV; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000000598; Chromosome C.
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: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..53
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 54..570
FT /note="5-aminolevulinate synthase, mitochondrial"
FT /id="PRO_0000001241"
FT ACT_SITE 359
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 284
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 312
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 356
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 388
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 389
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 474
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT MOD_RES 359
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT CONFLICT 332
FT /note="A -> R (in Ref. 1; CAA63497)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="T -> S (in Ref. 1; CAA63497)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 62139 MW; CD9151C4A529AA89 CRC64;
MESVIRSSAK ICPFMHSATG SMQSVKALKN ANLPAIAQQC PFMGKAMEQR RGYASSASGA
SAAAAATATA STSASNSNSS VEASASADVV DHATKEASFD YQGLFDSDLA KKRMDKSYRF
FNNINRLAKE FPMAHRKLED DKVTVWCSND YLALSKNQEV IEVMKKTLDK YGAGAGGTRN
IAGHNKHALQ LEAELATLHK KEGALVFSSC FVANDAVISL LGQKIKDLVI FSDELNHASM
IVGIKHASTK KHIFKHNNLD QLEELLAMYP KSTPKLIAFE SVYSMSGSVA DIDKICDLAE
KYGALTFLDE VHAVGLYGPH GAGVAEHCNF DAHRKAGIAS PEFRTVMDRV DMITGTLGKS
FGTVGGYVAG SLQLIDWVRS YAPGFIFTTT LPPAVMAGAA EAIRYQRSHL DLRQDQQRHT
TYVKDGLADL GIPVMPNPSH IVPVLVGNPH LAKQASDILM DKHRIYVQAI NFPTVARGTE
RLRITPTPGH TNDLSDILMD ALEDVWSTLQ LPRVRDWEAQ GGLLGVGDPN HVPQPNLWTK
DQLTLTNNDL HPNVKQPIIE QLEVSSGIRY
