ID A0A0F9ZQN3_TRIHA Unreviewed; 566 AA.
AC A0A0F9ZQN3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=THAR02_05319 {ECO:0000313|EMBL:KKP02587.1};
OS Trichoderma harzianum (Hypocrea lixii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP02587.1, ECO:0000313|Proteomes:UP000034112};
RN [1] {ECO:0000313|Proteomes:UP000034112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA Pe M.E., Sarrocco S., Vannacci G.;
RT "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT T6776.";
RL Genome Announc. 3:E0064715-E0064715(2015).
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:KKP02587.1}.
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DR EMBL; JOKZ01000144; KKP02587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9ZQN3; -.
DR OMA; DPHKMGL; -.
DR OrthoDB; 3024111at2759; -.
DR Proteomes; UP000034112; 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:UP000034112}.
FT MOD_RES 354
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 566 AA; 61796 MW; 17209EC7228F1F5A CRC64;
MPGSSRIPQS LRGSQLHWIG LIVADALLFS PTNSLKNIIF FYFVLRWTRR LWWKLKGRGI
IGAILELYRD VERTLYGYFL RAPGVRGQVQ KKVKESLDKM SNKLVPAGQT KYLSLPKEGL
TDEAVRAELD SLANMDHTRW EDGYVSGAVY HGEGDLLKLQ TEAFGKFTVA NPIHPDVFPG
VRKMEAEIVS MVLNLFHAPV GAAGVTTSGG TESILMAVLA ARQRAYNERG VTEPEMILPA
TAHTAFRKAG EYFKIKIHYV DCPAPTYQVD VRRVARLINR NTVLLVGSAP NFPHGIIDDI
SALSKLALRK KLCLHVDCCL GSFVIACLDK AGFETQPFDF RLKGVTSISC DTHKYGFAPK
GSSTVLYRSA ELRSYQYFVS PDWAGGVYAS PGLAGSRPGA LIAGCWASMM RLGETGYVDA
CGKIVGATKK ITEAIQNGPV LSSELEVLGK PLVSVVAFSA KNLDVYDIAD GMSSKGWHLN
ALQSPPAIHV AVTMPIVKVW ERLVSDLETV VEEEREKERV RLVEGKGAKG KAMGDSAALY
GVAGSLPNKG VVVDLATGFL DLLYKV
//
