ID H0A3B5_9PROT Unreviewed; 550 AA.
AC H0A3B5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Thiamine pyrophosphate protein {ECO:0000313|EMBL:EHL99151.1};
GN ORFNames=HMPREF9946_03307 {ECO:0000313|EMBL:EHL99151.1};
OS Acetobacteraceae bacterium AT-5844.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHL99151.1, ECO:0000313|Proteomes:UP000003292};
RN [1] {ECO:0000313|EMBL:EHL99151.1, ECO:0000313|Proteomes:UP000003292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT-5844 {ECO:0000313|Proteomes:UP000003292};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) 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:EHL99151.1}.
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DR EMBL; AGEZ01000097; EHL99151.1; -; Genomic_DNA.
DR AlphaFoldDB; H0A3B5; -.
DR STRING; 1054213.HMPREF9946_03307; -.
DR PATRIC; fig|1054213.3.peg.3036; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_4_5; -.
DR OrthoDB; 4494979at2; -.
DR BioCyc; ABAC1054213:G1H32-3067-MONOMER; -.
DR Proteomes; UP000003292; 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:UP000003292};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 191..325
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 550 AA; 59317 MW; AFC82AE7CE6B5C06 CRC64;
MSARTGGQIL VDQLVAQGVE RVTCVPGESY LAVLDALYDA KIDVLTCRQE GGAAIMAEAY
GKLTGRPGVC FVTRGPGATN ASHGVHIAMQ DSTPMILFVG QIETGMRERE AFQELDYRAV
FGSMTKWTTE IDTPDRIPEL VARAFRVAMQ GRPGPVVIAL PEEMLVALAE VPDVPRVEPA
TPAPAPADVT ALEKLLEGAK KPIAILGGSG WDEAAIDAMA DFADRWSLPV CTSFRRADRF
RWDHRCYVGD LGIGPSPKLS AMVKEADVLL LIGGRMSEMP SSSYTMIDIP VPQQTLVHVH
PGAEELGRVY APTIAIPVPP RAFTPALASL SPKGMPAWAD ATAEAHAAYL DWSGKTRKLP
GDFQYGEVVR WLNENLPADT VLCNGAGNFA GWMHRHWRFS QLGTQLAPTS GSMGYGVPAA
IMAKRQKPGS TSIVIAGDGD FLMNGQEFAT AVQHDIPFIV IVIDNGMYGT IRMHQERDYP
GRVSATRLKN PDFAAYAKAF GGHGEVVRRT EEFAPAFQRA VESGKPAILH CFLDPRALSV
GKDMPEGAPL
//