ID B2JJ84_PARP8 Unreviewed; 566 AA.
AC B2JJ84;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Thiamine pyrophosphate protein domain protein TPP-binding {ECO:0000313|EMBL:ACC72186.1};
GN OrderedLocusNames=Bphy_3016 {ECO:0000313|EMBL:ACC72186.1};
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC72186.1, ECO:0000313|Proteomes:UP000001192};
RN [1] {ECO:0000313|Proteomes:UP000001192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC {ECO:0000313|Proteomes:UP000001192};
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP001043; ACC72186.1; -; Genomic_DNA.
DR RefSeq; WP_012402364.1; NZ_CADFGH010000011.1.
DR AlphaFoldDB; B2JJ84; -.
DR STRING; 391038.Bphy_3016; -.
DR KEGG; bph:Bphy_3016; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_4_4; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000001192; Chromosome 1.
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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001192};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 12..127
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..335
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 394..540
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 566 AA; 61648 MW; 49606EB2B1D5EA87 CRC64;
MSLSSDASNM TTGARLMVDA LLTHGVERVF CVPGESFLAI LDSLHDETSQ IQTVVCRHEA
AAANMAEAVG KLTGRPGIAI VTRGPGATHA SIGVHTAFQD STPMILLIGQ CAREHLDREA
FQEIDYRRMF GQMAKWVAQI DDARRIPEYM SHAFHVATSG RPGPVVLSLP EDMLSDACAA
MPGAPAYQRV AAAPAPQQIE RLRGLLEGAK KPMVIAGGSG WTPQACEDLR TFIENWQLPI
GLAFRFQDTL DNEHPNYAGD VGLGINPALA KRIQDADVLL ALGPRLGEAT TNGYTLLDIP
KTKQTLIHVH QGADELGRVY AADLPIVSGM PEIASMLAAL KRVAQPAWSG SAKEAHDAYL
EWRKPRMVPG DVQLGEIMLQ LREHLPKDAI LTNGAGNYAT WLHRHFAYRH FRSQLAPTSG
AMGYGVPAAI AAKSMYPDRT VVAFAGDGCF MMSSSEIATA VQYDLPVIFI VVNNSQYGTI
RMHQERHYPN RVHGTGLTNP DFAAFARSFG AHGETVERTE DFMPAFKRAQ ESKKPAVIEV
RMIQEASTPG ATLEQVREQG RKLRGE
//
