ID A8TMS1_9PROT Unreviewed; 515 AA.
AC A8TMS1;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Death domain-containing protein {ECO:0000259|PROSITE:PS50017};
GN ORFNames=BAL199_03554 {ECO:0000313|EMBL:EDP65869.1};
OS alpha proteobacterium BAL199.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP65869.1, ECO:0000313|Proteomes:UP000003417};
RN [1] {ECO:0000313|EMBL:EDP65869.1, ECO:0000313|Proteomes:UP000003417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL199 {ECO:0000313|EMBL:EDP65869.1,
RC ECO:0000313|Proteomes:UP000003417};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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:EDP65869.1}.
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DR EMBL; ABHC01000003; EDP65869.1; -; Genomic_DNA.
DR AlphaFoldDB; A8TMS1; -.
DR STRING; 331869.BAL199_03554; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 9773408at2; -.
DR Proteomes; UP000003417; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd02002; TPP_BFDC; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF86; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVX-RELATED; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000003417}.
FT DOMAIN 473..515
FT /note="Death"
FT /evidence="ECO:0000259|PROSITE:PS50017"
SQ SEQUENCE 515 AA; 53622 MW; 2384B94993395D2E CRC64;
MNGAESLVRT LVASGVDVCF TNPGTSEMHF VAALDRVDGM RCVLGLFEGV VTGMADGYGR
MADKPASTLL HLGPGLGNGI ANLHNAKKGF TPIVNIVGEH ATYHIKYDAP LTSDIEGIAR
PVSGWVKTST DAKDVAGDGA AAVAASMGPP GQIATLILPA NTAWDESNGP AAPVAPTPLP
GPDADAVREA AKALKAGGKA LLHMTGRSLR ADTLEIAGRI AAKTGCRLSC QTSNGRWQRG
AGRVSIERIQ YPVDIALKQL ASVEQLVLLG TKAPVAFFAY PNKPSLLTPE GCAVHTLAEI
GDDHLAVLTA LCDELDAWNA KPVLQQAERP ELATGALTPE AVAAALGRLM PENAIIADES
VTSGRGFMPY TAGSAPHDWL SLTGGAIGLG LPYATGAAIA CPDRKVICTE GDGSGMYTLQ
ALWTQAREGC DVVNIIFANR SYAILRHELT NVGAQNPGRK AIDMLTLDRP ELDWVALAKG
MGVAGVRVDT AEAFNDALAR AIAEPGPHLI EAWMA
//