ID A0A167AAC7_9PEZI Unreviewed; 586 AA.
AC A0A167AAC7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
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};
DE Flags: Fragment;
GN ORFNames=CI238_02344 {ECO:0000313|EMBL:KZL79895.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL79895.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL79895.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL79895.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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:KZL79895.1}.
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DR EMBL; LFIW01002021; KZL79895.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167AAC7; -.
DR STRING; 1573173.A0A167AAC7; -.
DR Proteomes; UP000076584; 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: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:UP000076584}.
FT MOD_RES 374
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZL79895.1"
SQ SEQUENCE 586 AA; 64301 MW; 9D0426A45459A292 CRC64;
LPLSRNIAPR YAKLHITADK MPGSSRIPAS LREGLNQVKR SRQATPLLVL NLDLLRNVIF
FLFLWRWTRK AFLKLKGRGL IGSIVELYID IRRVLYGYFL RAPGVRGQVQ KQINESMTKL
QAKMIPANLT RYLTLPKEGM SEDDVRKELD TLANMDHTRW EDGFVSGAVY HGEEELIKLQ
TEAFGKFTVA NPIHPDVFPG VRKMEAEIVS MVLSMFNAPP GGAGATTSGG TDSILMACLS
ARQRGYFEKG ITEPEMILPE TAHTAFRKAG DYFKIKIHYV ACPAPNYQVD VRAVSRLINS
NTILLVGSAP NFPHGIIDDI SALSKLALKK KLCLHVDCCL GSFMVPFLDK AGFETELFDF
RLKGVTSISC DTHKYGFAPK GNSTVLYRSA ELRKYQYYVS PDWSGGVYGS PGMAGSRPGA
LIAGCWASLM NVGEAGYIDA CVKIVGTAKK IAERIRETPA LDTELEILGK PLVSVVAFTA
KNLNVYDIAD GMSEKGWHLN ALQSPPAIHV AVTLPITKVY DKLLTDLEAV VEAEKEKERV
RVVEGKGPKG KAVGDSAALY GVAGSLPNKS VVVDLANGFL DLLYKA
//
