ID A0A165G875_EXIGL Unreviewed; 1112 AA.
AC A0A165G875;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=PLP-dependent transferase {ECO:0000313|EMBL:KZV90126.1};
GN ORFNames=EXIGLDRAFT_720698 {ECO:0000313|EMBL:KZV90126.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV90126.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV90126.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV90126.1,
RC ECO:0000313|Proteomes:UP000077266};
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|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50};
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; KV426056; KZV90126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165G875; -.
DR STRING; 1314781.A0A165G875; -.
DR InParanoid; A0A165G875; -.
DR OrthoDB; 1607139at2759; -.
DR Proteomes; UP000077266; 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; 3.40.640.10; 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 PANTHER; PTHR42735; -; 1.
DR PANTHER; PTHR42735:SF4; TYROSINE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Transferase {ECO:0000313|EMBL:KZV90126.1}.
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 521
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 1112 AA; 123438 MW; 1BF8AD0BB2B5DB90 CRC64;
MSMRSAVPRG DVVDDPSKRG NTPSADAVRL SRGPAAHQHG HAYEPQSTNN MHNAVASWFL
GPQGESKERL KDLFEKIVES TAAGRLAYHE EDGAFVSTDM MQSQQFSEES QRLEHLLKNF
TDLLNKYSVP FFSQRYAGHM CFETSLPAIL GYLSTIMTNP NNVAFEASPF TTIVEITVGQ
QLCEMLGYSC KVGEEFCKLQ GHFPDLCDDG RTCAKCTQIG VSAEERDESA WGHITCDGSV
ANTESMWVAR NLKFYPLSLR LAMEKDKLLG SAAAGLKLPT CENPEKPVLF TSLNAWQLLN
LRTNVILDLS TLLNTQCGIS PEYSEQAMKK YLVQEMGKDA LMAEFTATFK TEPLKQPQYL
ISATRHYSWP KAAALTGIGA MNLVSIPVDV HARLKIDVLR KQLQQRFDDK VPVYAVVAVI
GTTEEGAVDP LDEVLKLKDE FQAKGMSFVV HADAAWGGYF ASMIREPPAP PQPPVGHLPV
GLPDPHRGPI DPVPEFSMRK HTELQFRALA RTDSITIDPH KSGYIPYPAG GLCYKDGRMR
QLVTWSAPYL SMGSQTESIG VFGVEGSKPG AAAAAVFLHH QMVGLHKRGH GALLGEVMWT
SSRMSAHWAT LSDETTEFTV VPFNEVDANQ MRIIRDKIIG KDNATVLKDK EACEALRELG
SDLNINAFGC NFRVGGITNS DVEEANILGS CIYKALSIAD EPRDVKEVPM FLSSSTFKMD
EYGECAEALK KRMGLETASG QDVFVLRNVA MSPFQSSGGF VEEIARIFRV AVEKLLPPFI
KRNTIKALQH NFVVQGTAET GKTIHLVYLP NFYDANCRYQ LILSVDVLQV KPGAQIPPDE
RITGIPTMCS IEDTTIKDIV SGEKLRAVVT KSSTSHREDV ILGNVRVVKN RSLSSAHRDL
AYPEYIHSYL YGTLEEPYMD HAIVRAPNWQ LTATKPVELD LEKPLTVEQL KEGVIVKFVT
VPERAYQPLG EAAFRKMFRV GEFWDVEVYK DPNPATAHRS GLLDMRKAVL ITKGKLASTQ
WPWVWEGLNA AREPWVKGKL IERPRTLTEL LHVLPPVKEP PEPTARRGGA MPVARKMPMG
RVEHTTTNSH SKLFGRSRQE TWADVISRVA SM
//