ID F9F7S5_FUSOF Unreviewed; 519 AA.
AC F9F7S5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOXB_02450 {ECO:0000313|EMBL:EGU87056.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU87056.1};
RN [1] {ECO:0000313|EMBL:EGU87056.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU87056.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
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.
CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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:EGU87056.1}.
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DR EMBL; AFQF01000749; EGU87056.1; -; Genomic_DNA.
DR AlphaFoldDB; F9F7S5; -.
DR STRING; 660025.F9F7S5; -.
DR PaxDb; 5507-FOXG_05210P0; -.
DR GO; GO:0016831; F:carboxy-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; 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 InterPro; IPR021115; Pyridoxal-P_BS.
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.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 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}.
FT REGION 11..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 317
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 519 AA; 56433 MW; 03CA104329C64510 CRC64;
MSDLFNLDVQ RTRLSRRHGP EPGSAPAPTL PELSAIQTAE AKLPRPDSED YLRGVSQEDV
VRHIIRDIIP ACNGQGSSSR YYGFVTGGTL PIAEWADNVV SRLDQNVQVH LPAQTIATTL
EDAALEMLVS LLRLGDWRGR TFTTGATGSN VLGLACGREA ILEERGQSIG EVGLLAACLS
AGIRELQILT SAGHSSLSKA ASVVGFGRGA VKELRLSDSE PWRLDLEALE RELQKKDTAS
VIALSAGEVN TGRYALTGVE EMRKVRELAD RYGAWIHVDG AFGIFARALP EEDDYKILRN
RVEGIELADS ITVDGHKLLN VPYDCGMFLT RSPAILQSVF TNPNAAYLST GGASTIPSPL
NVGLENSRRF RALPAYAVLL SEGRPGMANL LANMTALSRQ VAAFLRGSEH YELLPDDGAN
FNEIFMIVLF RAKKSSLNDE LVQKINATRQ MYVGVEEWGV DKHEHTDTPA GSATYYAYAS
VDTRSKIGIF ESANISKTVS DNVEIYTPKT KMIIYSTAG
//
