ID   A0A2B7ZH39_9EURO        Unreviewed;       573 AA.
AC   A0A2B7ZH39;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=GX50_04538 {ECO:0000313|EMBL:PGH32691.1};
OS   Emmonsia crescens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX   NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH32691.1, ECO:0000313|Proteomes:UP000226031};
RN   [1] {ECO:0000313|EMBL:PGH32691.1, ECO:0000313|Proteomes:UP000226031}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH32691.1,
RC   ECO:0000313|Proteomes:UP000226031};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-2017) 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   -!- 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:PGH32691.1}.
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DR   EMBL; PDND01000085; PGH32691.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7ZH39; -.
DR   STRING; 73230.A0A2B7ZH39; -.
DR   VEuPathDB; FungiDB:EMCG_03724; -.
DR   VEuPathDB; FungiDB:EMCG_05302; -.
DR   OrthoDB; 3024111at2759; -.
DR   Proteomes; UP000226031; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000226031};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        25..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   MOD_RES         360
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   573 AA;  62070 MW;  FA1982BF46E4A315 CRC64;
     MSSNAMLPVA LQNKLMSARR SSSGIFSSAS FNLIRNVFFF LFLFRLARKS FYTIRGHGPL
     GTIRNAYSYI RLVFYSLFLR APGVRGQVDK QVTTALTKLE AKLAPQTPGI LKNTGLPKQG
     WSHDRVRAEL DKLAGMEHTK WEDGRVSGAV YHGGDELVGL QTTAFGQFAV TNPIHPDVFP
     GVRKMEAEVV AMVLGLFNAP DGGAGVTTGG GTESILMACL SARQKAYVER RVTEPEMIIP
     CTAHAAFNKA CQYFGIKLHT VPCPGPDYKA DIRAIRRLIN PNTILLVGSA PNFPHGIVDD
     IPALSRLAIK HKIPLHVDCC LGSFVIAFLK RAGYPSPYEE QGGFDFRLPG VTSISVDTHK
     YGFAPKGNSV VLYRNRTLRS YQYFILPNWP GGVYASPSIA GSRPGALIAG CWSSLMAIGE
     SGYIDSCHQI IAAAHTLEQA IREHPSLSTA LTVIGKPMVS VVSWASVTPD IDIYDIADML
     SAKGWHLNAL QSPPAMHMAF TVPTAAAVEK LIADLVSVVE QERAKAAERK RLGLKVQKGK
     GDASALYGVA GSIPDKSIVN RLAEGFLDTL YLA
//