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Database: UniProt
Entry: A0A0Q5YRA1_9BRAD
LinkDB: A0A0Q5YRA1_9BRAD
Original site: A0A0Q5YRA1_9BRAD 
ID   A0A0Q5YRA1_9BRAD        Unreviewed;       202 AA.
AC   A0A0Q5YRA1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Thiamine pyrophosphate enzyme TPP-binding domain-containing protein {ECO:0000259|Pfam:PF02775};
GN   ORFNames=ASG57_08740 {ECO:0000313|EMBL:KQT08253.1};
OS   Bradyrhizobium sp. Leaf396.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1736363 {ECO:0000313|EMBL:KQT08253.1, ECO:0000313|Proteomes:UP000051536};
RN   [1] {ECO:0000313|EMBL:KQT08253.1, ECO:0000313|Proteomes:UP000051536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf396 {ECO:0000313|EMBL:KQT08253.1,
RC   ECO:0000313|Proteomes:UP000051536};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT08253.1, ECO:0000313|Proteomes:UP000051536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf396 {ECO:0000313|EMBL:KQT08253.1,
RC   ECO:0000313|Proteomes:UP000051536};
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   -!- 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:KQT08253.1}.
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DR   EMBL; LMQJ01000045; KQT08253.1; -; Genomic_DNA.
DR   RefSeq; WP_024339886.1; NZ_LMQJ01000045.1.
DR   AlphaFoldDB; A0A0Q5YRA1; -.
DR   OrthoDB; 8218035at2; -.
DR   Proteomes; UP000051536; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd03372; TPP_ComE; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR022494; Sulfopyruvate_deCO2ase_bsu.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR42818:SF1; SULFOPYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR42818; SULFOPYRUVATE DECARBOXYLASE SUBUNIT ALPHA; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        53..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          42..170
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   202 AA;  21836 MW;  999849E5CE5D0388 CRC64;
     MNTDVSARNT KVMNRFDVTS RLITKLKHEE AVIGGIGNTN FDLWAAGHRP QNFYMLGSMG
     LAFPIALGVA LAQPERRVFA LEGDGSLLMQ LGALSTIATL KPENLTMIVM DNGIYQITGA
     QPTPAANVAD IVAIAIGSGL ANSAWAADEE DFERLVEEAL AAREPRLIAV RIDDKPGVGT
     TRRDPVQIRE LFMHGLGVRE PL
//
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