ID A0A1V2LCN2_CYBFA Unreviewed; 623 AA.
AC A0A1V2LCN2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Transaminated amino acid decarboxylase {ECO:0000313|EMBL:ONH69602.1};
GN ORFNames=BON22_0402 {ECO:0000313|EMBL:ONH69602.1};
OS Cyberlindnera fabianii (Yeast) (Hansenula fabianii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=36022 {ECO:0000313|EMBL:ONH69602.1, ECO:0000313|Proteomes:UP000189513};
RN [1] {ECO:0000313|Proteomes:UP000189513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=65 {ECO:0000313|Proteomes:UP000189513};
RX PubMed=28385833; DOI=10.1128/genomeA.00064-17;
RA van Rijswijck I.M.H., Derks M.F.L., Abee T., de Ridder D., Smid E.J.;
RT "Genome sequences of Cyberlindnera fabianii 65, Pichia kudriavzevii 129,
RT and Saccharomyces cerevisiae 131 isolated from fermented masau fruits in
RT Zimbabwe.";
RL Genome Announc. 5:E00064-E00064(2017).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR036565-2};
CC Note=Binds 1 Mg(2+) per subunit. {ECO:0000256|PIRSR:PIRSR036565-2};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:ONH69602.1}.
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DR EMBL; MPUK01000001; ONH69602.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V2LCN2; -.
DR STRING; 36022.A0A1V2LCN2; -.
DR VEuPathDB; FungiDB:BON22_0402; -.
DR OMA; AQEISVM; -.
DR OrthoDB; 1000728at2759; -.
DR Proteomes; UP000189513; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02005; TPP_PDC_IPDC; 1.
DR CDD; cd07038; TPP_PYR_PDC_IPDC_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR012110; PDC/IPDC-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047214; TPP_PDC_IPDC.
DR InterPro; IPR047213; TPP_PYR_PDC_IPDC-like.
DR PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43452:SF3; TRANSAMINATED AMINO ACID DECARBOXYLASE; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR PIRSF; PIRSF036565; Pyruvt_ip_decrb; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036565-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036565-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000189513};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 26..128
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 239..356
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 435..539
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 508
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 510
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 623 AA; 69658 MW; 1D88D35517F9296E CRC64;
MAPIPDASAP TPTTITTSTT MENNTMKFGE YLFKRLAQVH SVNSIFGVPG DFNLGLLDHL
YTTDLQWIGG CNELNSGYSA DGYSRYTNSL GVLITTYGVG ELSAINAVAG AFAEYSKVLH
IVGIPTRRAM FDNVEKKKHL HHLVPSLDSL EDSDHFVYTK MVGGISCIAK TITNPATAAE
DVDEVIKTIF KHSRPGYLFL PLDMADEIID ASRLITEPAV DFHRVKIEEE ANTKLVGDKI
LSKLYNSKIP AFLADVLVRR YDQGVELLRE LVNTTNIHNY TTFMGKSILN EYHPSFVGDY
IGIESNKGVK ENLESSDCIL YFGPHINEIN TGHYSFDFTE EQSILLHPDY IKVGSELFRG
VHMINVMRYL LSNIDTSRIA APVPVPYHVS PRYPNIPSRS SISQSVLLKK FESFLQEGDV
VVCETGSFMF GIPDFRFKTD VNYIAQGFYL SIGMALPCSV GVGIAMKDQG SKSRLILVEG
DGSAQMTIQE LSSFPHYGLK PIIFLLNNSG YTVERIIRGE NQTYNDIKPW NWSKVFELFE
YDGTAEGKLI SEKAKQNKHC VSSIVSSEEE LSLAMTSVNS KVDDDKLRFF EVILDKLDCP
WRFFHMNNYR LFPLTDAGSK ALA
//
