ID A0A085JCS4_9GAMM Unreviewed; 554 AA.
AC A0A085JCS4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Thiamine pyrophosphate-requiring enzyme {ECO:0000313|EMBL:KFD18270.1};
GN ORFNames=GTPT_2460 {ECO:0000313|EMBL:KFD18270.1};
OS Tatumella ptyseos ATCC 33301.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Tatumella.
OX NCBI_TaxID=1005995 {ECO:0000313|EMBL:KFD18270.1, ECO:0000313|Proteomes:UP000028602};
RN [1] {ECO:0000313|EMBL:KFD18270.1, ECO:0000313|Proteomes:UP000028602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33301 {ECO:0000313|EMBL:KFD18270.1,
RC ECO:0000313|Proteomes:UP000028602};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-2014) 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:KFD18270.1}.
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DR EMBL; JMPR01000038; KFD18270.1; -; Genomic_DNA.
DR RefSeq; WP_025901855.1; NZ_JMPR01000038.1.
DR AlphaFoldDB; A0A085JCS4; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000028602; 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 GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR CDD; cd02010; TPP_ALS; 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:SF129; ACETOLACTATE SYNTHASE; 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:UP000028602};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..122
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 195..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 387..532
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 554 AA; 60285 MW; 5D41B4F6625D0568 CRC64;
MTVKTKNVAE FLVSCLEAEG VKYVFGIPGE ENIKFVRAIT ASENIRFILV RHEQAASFMA
DIYGRLTGKA GVCTATLGPG AINLLLGTAD AQTDSSPLVA ISAQVGLNRI YKESHQIVDL
TAMFRPVTQW ADTLYTPAAS AEMVRKAFQI AQQERPGATY LAIPQDVEAM PVPENLQPIL
PVSSSISLPP AETVSAIAKL LREARYPVIL AGHGVARNGA ASALNQFTER YQIPAATTFM
GKGVISDRSQ HALGVMGFMR HDYENFAFDK ADVILAVGYE LQEFAPERMN PDADKKIIHI
NSFLPDTDRH YRTDIALAAD ISLTLSALSE ALGEEPLHAQ PGSATIRHLR EQELEKGRHD
DSFPLKPQRV VADMRSALDD HDIVLADTGA IKMWVSRLYP TYQPLTCLTS NGLSTMAFSL
PGAIAAKLAF PQRKVLASMG DGSFMMNSQE IETAVRERIP LVVLVWVDGS YGLIKWKMDI
EEGAHDSVDF GNPDFVKYAE SFGARGHQIT SAGELLPVLK EALAGDGVTV IACPVDYREN
MALVKTLGEL TIAL
//