ID D4XHM3_9BURK Unreviewed; 560 AA.
AC D4XHM3;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Thiamine pyrophosphate protein {ECO:0000313|EMBL:EFF73679.1};
GN ORFNames=HMPREF0004_4970 {ECO:0000313|EMBL:EFF73679.1};
OS Achromobacter piechaudii ATCC 43553.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=742159 {ECO:0000313|EMBL:EFF73679.1, ECO:0000313|Proteomes:UP000004510};
RN [1] {ECO:0000313|Proteomes:UP000004510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43553 {ECO:0000313|Proteomes:UP000004510};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R., Gibbs R.;
RT "Complete sequence of Mobiluncus curtisii ATCC 43063.";
RL Submitted (MAR-2010) 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:EFF73679.1}.
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DR EMBL; ADMS01000116; EFF73679.1; -; Genomic_DNA.
DR RefSeq; WP_006221117.1; NZ_GG770409.1.
DR AlphaFoldDB; D4XHM3; -.
DR PATRIC; fig|742159.3.peg.455; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_4_4; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000004510; 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; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 9..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 195..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..535
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 560 AA; 60569 MW; 43C67D77905A53D5 CRC64;
MSQQDSRLGG HILVDQLVAQ GVKHVFCVPG ESYLAVLDGL HDADIKVTVC RQEGGAAMMA
DAHGKLTGEP GICMVTRGPG ASNALAGVHI AKQDSTPMIL FVGQIERGMR EREAFQEMDY
RAVFGTQAKW VTEIDQVERI PELISRAFHI ATSGRPGPVV IALPEDMLVE AAKVADAPRY
ELIESAPTAG QLADLEKLLA DAKNPVAILG GTRWDARAVQ QFADFAQRHA LPTAVSFRRQ
MLFPADHPCF IGDVGLGINP ALLKRVADAD LILLVGGRMS ENPSQAYTLM DIPVPKQKLV
HVHPDTAELG RVYRATLAIN TSPAAFAESL GGLKAPAKPV WAEGTQAMRE SYLKWSDPAS
ITTPGALQMG QVMAYLEKTL PADAIMTNGA GNYATWLHRF HRFTRFGTQL APTSGSMGYG
LPAAVGAKRV WPDKTVVCFA GDGCFLMHGQ EFATAVQYDL PIIVVLVDNG MYGTIRMHQE
KHYPGRVSAT ELKNPDFADY ARAFGGHGER VETTDQFGPA FERALASGKP AILHCFIDPE
TITPSTTLEK IRDAALKAQH
//
