ID A0A0F2MBC8_SPOSC Unreviewed; 684 AA.
AC A0A0F2MBC8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=5-aminolevulinate synthase, mitochondrial {ECO:0000256|ARBA:ARBA00019560};
DE EC=2.3.1.37 {ECO:0000256|ARBA:ARBA00013257};
DE AltName: Full=5-aminolevulinic acid synthase {ECO:0000256|ARBA:ARBA00031691};
DE AltName: Full=Delta-ALA synthase {ECO:0000256|ARBA:ARBA00031945};
DE AltName: Full=Delta-aminolevulinate synthase {ECO:0000256|ARBA:ARBA00032773};
GN ORFNames=SPSK_02321 {ECO:0000313|EMBL:KJR86404.1};
OS Sporothrix schenckii 1099-18.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1397361 {ECO:0000313|EMBL:KJR86404.1, ECO:0000313|Proteomes:UP000033710};
RN [1] {ECO:0000313|EMBL:KJR86404.1, ECO:0000313|Proteomes:UP000033710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1099-18 {ECO:0000313|EMBL:KJR86404.1,
RC ECO:0000313|Proteomes:UP000033710};
RX PubMed=25351875; DOI=10.1186/1471-2164-15-943;
RA Teixeira M.M., de Almeida L.G., Kubitschek-Barreira P., Alves F.L.,
RA Kioshima E.S., Abadio A.K., Fernandes L., Derengowski L.S., Ferreira K.S.,
RA Souza R.C., Ruiz J.C., de Andrade N.C., Paes H.C., Nicola A.M.,
RA Albuquerque P., Gerber A.L., Martins V.P., Peconick L.D., Neto A.V.,
RA Chaucanez C.B., Silva P.A., Cunha O.L., de Oliveira F.F., dos Santos T.C.,
RA Barros A.L., Soares M.A., de Oliveira L.M., Marini M.M.,
RA Villalobos-Duno H., Cunha M.M., de Hoog S., da Silveira J.F., Henrissat B.,
RA Nino-Vega G.A., Cisalpino P.S., Mora-Montes H.M., Almeida S.R.,
RA Stajich J.E., Lopes-Bezerra L.M., Vasconcelos A.T., Felipe M.S.;
RT "Comparative genomics of the major fungal agents of human and animal
RT Sporotrichosis: Sporothrix schenckii and Sporothrix brasiliensis.";
RL BMC Genomics 15:943-943(2014).
RN [2] {ECO:0000313|EMBL:KJR86404.1, ECO:0000313|Proteomes:UP000033710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1099-18 {ECO:0000313|EMBL:KJR86404.1,
RC ECO:0000313|Proteomes:UP000033710};
RX PubMed=25480940;
RA Teixeira Mde M., Rodrigues A.M., Tsui C.K., de Almeida L.G.,
RA Van Diepeningen A.D., van den Ende B.G., Fernandes G.F., Kano R.,
RA Hamelin R.C., Lopes-Bezerra L.M., Vasconcelos A.T., de Hoog S.,
RA de Camargo Z.P., Felipe M.S.;
RT "Asexual propagation of a virulent clone complex in a human and feline
RT outbreak of sporotrichosis.";
RL Eukaryot. Cell 14:158-169(2015).
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:0000256|ARBA:ARBA00003076}.
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:0000256|ARBA:ARBA00001588};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from glycine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005029}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008392}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJR86404.1}.
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DR EMBL; AXCR01000006; KJR86404.1; -; Genomic_DNA.
DR RefSeq; XP_016589080.1; XM_016729193.1.
DR AlphaFoldDB; A0A0F2MBC8; -.
DR GeneID; 27664470; -.
DR KEGG; ssck:SPSK_02321; -.
DR VEuPathDB; FungiDB:SPSK_02321; -.
DR OrthoDB; 9643at2759; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000033710; Unassembled WGS sequence.
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 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 {ECO:0000256|ARBA:ARBA00023315};
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000256|ARBA:ARBA00023315}.
FT DOMAIN 249..603
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 128..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 684 AA; 72506 MW; 7D2D07E0A10EBF55 CRC64;
MDAVLRQSKA VCPFLKKASP ATLRALSTAS RQQAAPEASS ALIAASPCGG ALSKLQLLAG
RCPVMGKAMA VQATRIGTSR VAASSSMGYR GVAASLSAAF SMSAVASAPA ARAHGLHGSA
ARTCPHAASA TASTASSAPR TARLHTSRSQ EARAVDGHVF NDKRIPAGIP GADKVSKAAK
TAVAAGKAST TPGFAAAPAM AQTKFDYEGF YEAELDKKHK DKSYRYFNNI NRLAKDFPRA
HMADKEDRVT VWCANDYLGM GSNPQVLQTM HETLDEYGAG AGGTRNISGH NRHAVHLEET
VARLHAKESA LVFSSCYVAN DATLATLGSR MPGCVILSDS LNHASMIQGI RHSGTQKIVF
RHNDVEDLEA KLAALPLNVP KIIAFESVYS MCGSIGPIEA ICDLADKYGA LTFLDEVHAV
GMYGPNGAGV AEHLDFDAHV QGRPSGTLMD RIDIITGTLG KAYGCVGGYI AGSAQLVDMI
RSLAPGFIFT TSLPPATMAG ARTAIEYQMN YAGDRRLQQL HTRAVKESLA ARDIPVIPNP
SHIVPLLVGD AEVAKQASDM LLRDHQIYVQ SINYPTVPVG QERLRITPTP GHVKEFRDRL
VHAVDSIWTE LGIRRTSDWA RQVPGGFLGV GAPPAAENSP LWTDEQLGIT QAVRALQQQD
SHKDNGLTEA LLAQEKLSPV AATA
//
