ID   A0A0C9MMI3_9FUNG        Unreviewed;       549 AA.
AC   A0A0C9MMI3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=sphinganine-1-phosphate aldolase {ECO:0000256|ARBA:ARBA00038965};
DE            EC=4.1.2.27 {ECO:0000256|ARBA:ARBA00038965};
DE   AltName: Full=Sphingosine-1-phosphate aldolase {ECO:0000256|ARBA:ARBA00042568};
GN   ORFNames=MAM1_0061c03797 {ECO:0000313|EMBL:GAN04337.1};
OS   Mucor ambiguus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN04337.1};
RN   [1] {ECO:0000313|EMBL:GAN04337.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN04337.1};
RA   Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT   "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT   ambiguus NBRC6742.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC       1-phosphate lyase subfamily. {ECO:0000256|ARBA:ARBA00038302}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DF836350; GAN04337.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9MMI3; -.
DR   STRING; 91626.A0A0C9MMI3; -.
DR   OrthoDB; 3024111at2759; -.
DR   Proteomes; UP000053815; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 6.10.140.2150; -; 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; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR42735; -; 1.
DR   PANTHER; PTHR42735:SF6; SPHINGOSINE-1-PHOSPHATE LYASE 1; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053815};
KW   Transferase {ECO:0000313|EMBL:GAN04337.1}.
FT   MOD_RES         351
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   549 AA;  59791 MW;  5E8816062C27EEFA CRC64;
     MANAASRPSA LIRFTQLSNG VLDSRYLHHI KNIVFVLVLL NYWSKLYNTV LIGGPVRAVH
     DFKTYLIRIA FRQLRRLPAV QEKINKELGT TLAGMEKSMM DKEVGLGSNL TLPAKGMTEQ
     QVMESLHKFE GLKAADWAGG KVSGSIYHGG EDLTKILAEA YKIFAIANPL HPEIFPGIRR
     MEAESVAMVL SMYNAPSTGC GTMTSGGTES ILMACKTYRD MYKDLKGINY PEMVVPDTIH
     AAFMKAANYF KIKLITIPID PVTLKVDVKK MERAITKNTV MIAGSAVNFP HGIADDIVAL
     GKLAKKYKIG LHVDCCLGSF IMPFLEKAGF PTTDFDFRVD GVTSISCDTH KYGFAAKGSS
     IIMYRNATIR KYQYFLYSQW TGGIYASPSI AGSRPGALIA GCWSALMYMG EDGYLKACKD
     IVGARRIMEA GVRSIPQLHV KGDPIGPVLS FGANEPLNIY DVGDKLSARG WNLSALQNPS
     GLHISTTLPW VNSAETFVKD LKECVQGLVD DPSSGNGSTA AIYGTAASVP DKTIVDDVAA
     GFLDLLYKA
//