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Database: UniProt
Entry: A0A0Q5V7Y4_9ACTN
LinkDB: A0A0Q5V7Y4_9ACTN
Original site: A0A0Q5V7Y4_9ACTN 
ID   A0A0Q5V7Y4_9ACTN        Unreviewed;       548 AA.
AC   A0A0Q5V7Y4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Alpha-keto-acid decarboxylase {ECO:0000256|ARBA:ARBA00020054};
GN   ORFNames=ASG36_17955 {ECO:0000313|EMBL:KQS57137.1};
OS   Geodermatophilus sp. Leaf369.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=1736354 {ECO:0000313|EMBL:KQS57137.1, ECO:0000313|Proteomes:UP000051830};
RN   [1] {ECO:0000313|EMBL:KQS57137.1, ECO:0000313|Proteomes:UP000051830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf369 {ECO:0000313|EMBL:KQS57137.1,
RC   ECO:0000313|Proteomes:UP000051830};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS57137.1, ECO:0000313|Proteomes:UP000051830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf369 {ECO:0000313|EMBL:KQS57137.1,
RC   ECO:0000313|Proteomes:UP000051830};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Decarboxylates branched-chain and aromatic alpha-keto acids
CC       to aldehydes. {ECO:0000256|ARBA:ARBA00002938}.
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=a metal cation; Xref=ChEBI:CHEBI:25213;
CC         Evidence={ECO:0000256|ARBA:ARBA00001920};
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:KQS57137.1}.
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DR   EMBL; LMQA01000004; KQS57137.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q5V7Y4; -.
DR   STRING; 1736354.ASG36_17955; -.
DR   Proteomes; UP000051830; 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   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   PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43452:SF30; PYRUVATE DECARBOXYLASE ISOZYME 1-RELATED; 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:UP000051830};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          1..108
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          196..286
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          384..523
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   BINDING         432
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         459
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         461
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ   SEQUENCE   548 AA;  56232 MW;  2151C2F9EA9AAD68 CRC64;
     MSVAEYLGAR LLQAGVTDLF GVPGDFNLDL LDGLATVEGL AWVGSPNELG AGYAADAYAR
     VRGLAVLVTT YGVGELSAIN ALAGAAAEDA PLLHVVGSPR RAAVEAGALV HHTLADGEFG
     HFSRAAAELT VVTETLTLER AAEQIDTVVL AATTHRRPAY LSVPQDLALA RIDAGPLEHR
     LTAASDPAAL HAFESRVTEL LVDAQRPVLV VGQLVARFGL GADLADLAAR AGVAVVTQLS
     ARGVLDPEHP SFAGDHAGTM LDNGTAELVA AADVVVQVGT LLTSELTGFG SHRRPGADTP
     FLAATEAGFG ATATGRVLLP DALAALDRAL AGRRGPRFVR AGRPVAATPV HAPDAPLTQA
     ATWDLLAAAL PEHTALLADT GTAYWGAAAM PLPADTVFGG QPVWSSIGYA LPAVLGQGLA
     DRTRRPVLVI GDGAAQMTVQ ELSTIAAAGL APVVLLLDNR GYTIERALQS PRASYNDVAA
     WDWCALVPAL TGDRGRAVSV RTAGELSAAL ADAFADTTHL VFVQAHLDAD DTPPLIDALA
     RLATAAKG
//
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