ID A0A0Q4YDS7_9BURK Unreviewed; 566 AA.
AC A0A0Q4YDS7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KQP18144.1};
GN ORFNames=ASF43_09910 {ECO:0000313|EMBL:KQP18144.1};
OS Pseudorhodoferax sp. Leaf267.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736316 {ECO:0000313|EMBL:KQP18144.1, ECO:0000313|Proteomes:UP000051560};
RN [1] {ECO:0000313|EMBL:KQP18144.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP18144.1,
RC ECO:0000313|Proteomes:UP000051560};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP18144.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP18144.1,
RC ECO:0000313|Proteomes:UP000051560};
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 -!- 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:KQP18144.1}.
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DR EMBL; LMMV01000012; KQP18144.1; -; Genomic_DNA.
DR RefSeq; WP_056182539.1; NZ_LMMV01000012.1.
DR AlphaFoldDB; A0A0Q4YDS7; -.
DR STRING; 1736316.ASF43_09910; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000051560; Unassembled WGS sequence.
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; cd00568; TPP_enzymes; 1.
DR CDD; cd07035; TPP_PYR_POX_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; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 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 Reference proteome {ECO:0000313|Proteomes:UP000051560};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 197..332
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..539
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 566 AA; 60951 MW; 70EA1A607B8A35E9 CRC64;
MSKQIAGHLL VQCLVEQGVS HVFGVPGESY LAALDGFHAY GDRIQFVINR QEGGAAFMAE
AHGKLTGRPG VCFVTRGPGA TNASIGVHTA FQDSTPMVLF VGDVASDSRD REVFQEVDYQ
SFFGPSTKGF AKRVERIDDA RRIPEYVARA FATAMNGRPG PVVLVLPEDM LVQEVDVAPL
ARVEPVQAWS DPGALRTLRE MLLASKQPFV IAGGSGWTPQ SAQALQRFAE NWKLPVGNAF
RFQDTFDNWH PLYAGDVGIG LNPKLAQRIK DSDLVIAIGP RLGEMTTGGY TLLQAPKAKQ
KLVHIHSSAE ELNRVYQADL AINATMNAAA RSLEVLTAPT ELPWEEWARA ANADYVENLQ
PQALPGDIDM PAIIGLLQKH LPDDAVVTNG AGNFASWMHR FFRHHGLAKG HKTQLAPTNG
AMGYGVPAAI AAAITTGRTA FTIAGDGDFM MNGQELATAM QCGAKSIVLL LNNGMFGTIR
MHQEREYPRK VSGTALANPD FVKLAQAYGY AGVRITATAE FEAQLLAALE RPEGTLIEVV
LDPEVITTRG TLTAITQAAL NKAGQA
//
