ID A0A167LBK8_CALVF Unreviewed; 491 AA.
AC A0A167LBK8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=PLP-dependent transferase {ECO:0000313|EMBL:KZO95521.1};
GN ORFNames=CALVIDRAFT_499805 {ECO:0000313|EMBL:KZO95521.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZO95521.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZO95521.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZO95521.1,
RC ECO:0000313|Proteomes:UP000076738};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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DR EMBL; KV417288; KZO95521.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167LBK8; -.
DR STRING; 1330018.A0A167LBK8; -.
DR OrthoDB; 51460at2759; -.
DR Proteomes; UP000076738; 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; 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; PTHR11999:SF165; DECARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04980)-RELATED; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 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:UP000076738};
KW Transferase {ECO:0000313|EMBL:KZO95521.1}.
FT MOD_RES 302
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 491 AA; 52535 MW; B1FAEDCCB1FF8FDA CRC64;
MSGDLLSSLD AHTRAHLASL RTLPPTADPV KLRTALESLP TSLPEKGWGD ARTLEYLNGT
VAGGLAQGQA GPRYWGFVTG GVLPIAQAAD NLVTLYDQNV QVHLPTQSLS TVIESRTLEL
LLSLLSLNPA DFPGRTFTTG ATTSNILGLA CGRQWAIAKA HPGYSVAEDG FSGYGCKVFV
AKAHASLVKA ASVVGIGRKN VIECGKDVDE NGGLPFDLVR LESLMRECKE RGDGIIVSPG
FGEVNTGGFT PNIPKIRELC DRFGAWLHVD GAFGAFAKLV PDLQSYVEHL HLADSITVDA
HKWLNVPYDS AAFFTRQADV LPSVFGPSPA TGGPAYLASG PAGPSYPALD VVQSIPSPLN
VNLENSRRFR ALPVFAALLS LGREGYAELI QRNVAFAREL GEYIAAHESY ELLNPGNKVL
LNIVLFRAKM VDSNELLRRI NASGKMYASP TSWAGKGAVR IAVSNWMTRM DRDGKAASDL
EIALEVLDSV I
//
