ID E8RLG4_ASTEC Unreviewed; 544 AA.
AC E8RLG4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Thiamine pyrophosphate TPP-binding domain-containing protein {ECO:0000313|EMBL:ADU13708.1};
GN OrderedLocusNames=Astex_2046 {ECO:0000313|EMBL:ADU13708.1};
OS Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / KCTC 12464 /
OS NCIMB 9791 / VKM B-1370 / CB 48).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=573065 {ECO:0000313|EMBL:ADU13708.1, ECO:0000313|Proteomes:UP000001492};
RN [1] {ECO:0000313|Proteomes:UP000001492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15261 / DSM 4724 / KCTC 12464 / NCIMB 9791 / VKM B-1370 /
RC CB 48 {ECO:0000313|Proteomes:UP000001492};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Brun Y.V., Woyke T.;
RT "Complete sequence of chromosome 1 of Asticcacaulis excentricus CB 48.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP002395; ADU13708.1; -; Genomic_DNA.
DR RefSeq; WP_013479536.1; NC_014816.1.
DR AlphaFoldDB; E8RLG4; -.
DR STRING; 573065.Astex_2046; -.
DR KEGG; aex:Astex_2046; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_4_5; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000001492; 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; 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:UP000001492};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 189..320
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 378..524
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 544 AA; 58680 MW; FD0B85EB11AA5F8F CRC64;
MRTGGQILVD QLKRNGVERL TCVPGESYLA ALDAMYDADI DVLICRHEGG AAMMAEAYGK
LTGRPGICFV TRGPGATNAA HGVHIAQHDS TPMILFVGQV ERAFLGRGAF QELDYVAAFG
GIAKWVVEIS DPKRIPEIVA RAFRVAMQGR PGPVVVSLPE DILTEVVEVA DAPPVAAVAA
APTRADMAAF VQAVEAAERP MMILGGSRWT AEGCIAVAEF AARYDIPVAT EFRRTSLFAA
HHPCYAGDLG FGQNPALSQR VKDADLLILL GARMAEVPSN GYTLIGQQTL VHVFPEAEEI
GRVYQPALGI VSTPDQFAKT LSGISEAPPV QIIRGAAAHQ DWLKWTTTPS PIPGDFQYGE
VMVWLREHLP PETIITNGAG NYAIWVHRYW RHERPFTQVA PTSGSVGYSV PAGIMAKRQC
PDAPVVTFAG DGCFLMNGNE FATAVQYGIP LIIIVIDNGM WGTIRMHQER EYPHRPIGTE
LKNPDFAAYA KAFGGHGETV HTTADFAPAF ERARASGKPA ILHCLIDPQA ITPAKTLDQV
SRGE
//
