ID I3ZXU8_ORNRL Unreviewed; 580 AA.
AC I3ZXU8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Thiamine pyrophosphate-dependent enzyme, possible carboligase or decarboxylase {ECO:0000313|EMBL:AFL96532.1};
DE EC=1.2.5.1 {ECO:0000313|EMBL:AFL96532.1};
GN OrderedLocusNames=Ornrh_0314 {ECO:0000313|EMBL:AFL96532.1};
OS Ornithobacterium rhinotracheale (strain ATCC 51463 / DSM 15997 / CCUG 23171
OS / CIP 104009 / LMG 9086).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Ornithobacterium.
OX NCBI_TaxID=867902 {ECO:0000313|EMBL:AFL96532.1, ECO:0000313|Proteomes:UP000006051};
RN [1] {ECO:0000313|EMBL:AFL96532.1, ECO:0000313|Proteomes:UP000006051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51463 / DSM 15997 / CCUG 23171 / LMG 9086
RC {ECO:0000313|Proteomes:UP000006051};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Mikhailova N., Teshima H., Kyrpides N., Mavromatis K., Pagani I.,
RA Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Lang E., Kopitz M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Ornithobacterium rhinotracheale DSM 15997.";
RL Submitted (JUN-2012) 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; CP003283; AFL96532.1; -; Genomic_DNA.
DR RefSeq; WP_014790162.1; NC_018016.1.
DR AlphaFoldDB; I3ZXU8; -.
DR SMR; I3ZXU8; -.
DR STRING; 867902.Ornrh_0314; -.
DR GeneID; 71568590; -.
DR KEGG; orh:Ornrh_0314; -.
DR PATRIC; fig|867902.3.peg.315; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_10; -.
DR OMA; YEATHEC; -.
DR Proteomes; UP000006051; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0052737; F:pyruvate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 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; IPR047211; POXB-like.
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; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 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 Ligase {ECO:0000313|EMBL:AFL96532.1};
KW Oxidoreductase {ECO:0000313|EMBL:AFL96532.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006051};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..114
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 191..319
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..528
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 580 AA; 63681 MW; F8D639D6FAA2083D CRC64;
MAKRVADQLV EMLVEAGVKR VYGITGDSLN PVNDAIRNDG RLEWVHVRHE EAGAYAASMD
AELNGIGCCM GSSGPGHVHL INGLYDANRA GNPVIAIAST CPSNKFGQEY FQETNPFYLF
QDCSKYVYVA NTPTQFPHMM QHAIQAAIEQ KGVAVVGLPG DVAAAEANDI ITSQKNYKTE
SVYLPSDAQL DTLAELLNQN KKISLYCGHG CRHAVPEVMA LAEKLKAPMA YSFRGKIFFD
RVDNPYATGL NGLLGHRSGY LTCNDADVLV MLGTDFPYAE FLPQKIKIVQ IDEKPSRIGR
RAKVDIGLAG DIKDTINALL PKLKGNDSDE FLKKMQKEYK ESEDALERFV KEDSTKTDEI
QPEYVAHVIN ELAEDDAIFT VDTGMTSVWA ARFIKGKRGR YLTGSFNHGS MANAMPMSIG
AAGAAPHRQV VAMCGDGGIS MLLGDLATIM QYKLPIKIIV FNNRSLGMVK LEMQVAGYVD
WQTDMVNPEF DKIGELMGMK GIAVHKTSEV ESAIKEAFEH DGPALVNIYT NPNSLAMPPH
ITLQQMKGFT TSMFKKLAEG KFGDIEQSIS SNIKHLTELF
//