ID V4RTK4_9CAUL Unreviewed; 551 AA.
AC V4RTK4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Thiamine pyrophosphate protein {ECO:0000313|EMBL:ESQ94498.1};
GN ORFNames=ABENE_01360 {ECO:0000313|EMBL:ESQ94498.1};
OS Asticcacaulis benevestitus DSM 16100 = ATCC BAA-896.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1121022 {ECO:0000313|EMBL:ESQ94498.1, ECO:0000313|Proteomes:UP000017837};
RN [1] {ECO:0000313|EMBL:ESQ94498.1, ECO:0000313|Proteomes:UP000017837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16100 {ECO:0000313|EMBL:ESQ94498.1,
RC ECO:0000313|Proteomes:UP000017837};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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:ESQ94498.1}.
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DR EMBL; AWGB01000003; ESQ94498.1; -; Genomic_DNA.
DR RefSeq; WP_018082148.1; NZ_AWGB01000003.1.
DR AlphaFoldDB; V4RTK4; -.
DR STRING; 1121022.GCA_000376105_02481; -.
DR PATRIC; fig|1121022.4.peg.269; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000017837; 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:UP000017837};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 195..326
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 385..531
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 551 AA; 59765 MW; 0A612E5217D9E247 CRC64;
MTSRTGGQIL VDQLVKQGVE RVTCVPGESY LAALDAMHDA DIDVLICRHE GGAAIMAEAY
GKLTARPGVC FVTRGPGATN AAHGVHIAQH DSTPMILFIG QVERAMLGRG AFQEMDYQAF
FGSTAKWVVE ITDAKRIPEI VARAFRVAMQ GRPGPVVISL PEDVLTDIED VADAPVLSFA
KPELSVKALQ QFEVLLAKAK KPLVILGSSN WSLEGCQAIV NFAETFALPV ATEFRRSALF
PADHPSYAGD LGFGPNPKLA QRVKDADLLI LLGARMAEVP SSSYTLIDLP TPQQTLVHIF
PDAGEIGKVY QPALGNVCAP DAFAQSLADL KPPVTKPWLE ETQNAHMDFL MWTTTPAKIP
GDFQYGEVMV WLRENLPADT ITCNGAGNYA IWLHRYWRHN QPRTQIAPTS GSVGYSVPAG
VMAKRQCPDK TVVVFAGDGC FLMHGNEFAT AVQYDIPVIV LVIDNGMYGT IRMHQERNYP
HRVVGTDLKN PDFAAYAKAF GGHGETVRTT AEFAPAFQRA QASGKPAIIH CYIDPQAITP
AKTLDQIADG K
//
