ID A7IJ42_XANP2 Unreviewed; 572 AA.
AC A7IJ42;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Thiamine pyrophosphate protein domain protein TPP-binding {ECO:0000313|EMBL:ABS68035.1};
GN OrderedLocusNames=Xaut_2795 {ECO:0000313|EMBL:ABS68035.1};
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=78245 {ECO:0000313|EMBL:ABS68035.1, ECO:0000313|Proteomes:UP000002417};
RN [1] {ECO:0000313|EMBL:ABS68035.1, ECO:0000313|Proteomes:UP000002417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1158 / Py2 {ECO:0000313|Proteomes:UP000002417};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL Submitted (JUL-2007) 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; CP000781; ABS68035.1; -; Genomic_DNA.
DR AlphaFoldDB; A7IJ42; -.
DR STRING; 78245.Xaut_2795; -.
DR KEGG; xau:Xaut_2795; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_4_5; -.
DR OrthoDB; 4494979at2; -.
DR PhylomeDB; A7IJ42; -.
DR Proteomes; UP000002417; Chromosome.
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:UP000002417};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 9..125
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..330
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 394..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 572 AA; 60770 MW; 73E896B9E60C8B79 CRC64;
MQHSANIRSG GEILVDALKI HGVDTVYCLP GESFLPAIDA LAGATGRIRT IVTRHEAAAA
NMAEAYGKLT GRPGICFVTR GPGASHAAIG IHTAAQDSTP LILFIGQVDT AIRGREAWQE
VDYPAMFGGM AKWVVEVDRP ERLPELVSRA FHVAVSGRPG PVVVALPEDV LGASAQVADA
QAYKRIAAHP GADDLNRLTA MLEASERPLV IVGGGGWSAR ACRDFQHFVE DFDLPVAAAF
RRQDILDNHH PNYVGHAGLG PNPKLVARIR AADLIVAIGP RLGETTTAGY TLFELPRPAQ
RFVHVHADPL ELGRVYQADL PINAGMPEFA AAAAALKPRG AAGWHAPWSA AVKAARADYL
ADQTPGAMPG RLDLGAVMVH LRESLPRDAI LTNGAGNYAI WVHRFHRYGG FRTQLAPTSG
AMGYGLPAAI AAKLHQPARD VICFAGDGCF QMSGQELATG CQYGAGVVVL LVNNGIYGSI
RMHQEREYPG RVFATTLENP DFPALARAYG AFGERVEETA AFAEAFNRAR AFAADRNKPA
LLELVIDPEA ITPSATLTGL REAALKAGQG AT
//
