ID K9AUU2_9MICO Unreviewed; 550 AA.
AC K9AUU2;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Thiamine pyrophosphate central domain-containing protein {ECO:0000313|EMBL:EKU46327.1};
GN ORFNames=C272_12291 {ECO:0000313|EMBL:EKU46327.1};
OS Brevibacterium casei S18.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=1229781 {ECO:0000313|EMBL:EKU46327.1, ECO:0000313|Proteomes:UP000009879};
RN [1] {ECO:0000313|EMBL:EKU46327.1, ECO:0000313|Proteomes:UP000009879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S18 {ECO:0000313|EMBL:EKU46327.1,
RC ECO:0000313|Proteomes:UP000009879};
RA Sharma R., Singh A., Jangir P.K.;
RT "Genome Sequence of Brevibacterium casei S18.";
RL Submitted (SEP-2012) 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:EKU46327.1}.
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DR EMBL; AMSP01000010; EKU46327.1; -; Genomic_DNA.
DR RefSeq; WP_009379547.1; NZ_AMSP01000010.1.
DR AlphaFoldDB; K9AUU2; -.
DR PATRIC; fig|1229781.4.peg.2468; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 3203527at2; -.
DR Proteomes; UP000009879; 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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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:UP000009879};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..104
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 189..314
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 380..527
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 550 AA; 57422 MW; D881BC5A1EB7756F CRC64;
MAHTSAHVAH TLARHIDEVF GLMGNGNAYF LDSLLTTTSA NYTAVRHEAG AVVAADAHFR
TSGRIAAATT TYGAGFTNTL TALAEAAQAR VPLVLVVGDE PTSGPRPWDV DQIAMASAVG
VRTYTVGRVD AAAATVTAIE HALTYRVPVV LAIPYDVATL EIGEIPEVPG PGEPSPLSPT
GEFPQAALDR LTGLLAEAER PILLAGRGAW LAGAAKELGE LADATGALTV TTALGRNIFP
RSEYDLGVAG GFGAPGAMER VRQADVAVVI GASLNQFTMR FGELFAPGTQ VWQIDVDDRP
THARVGGFIR ADARLAAAEL TARLRAAGAR PSTWRESVDT TADRTYEAGT EFAADGRLDP
RAAAARLGEL LPEDRVVVSD GGHFIAWANM FWEPSAPDRL ALVGTAFQSI GLGWHSVAGA
ARANPEATIV LTTGDGGGMM ALSDLDTAIR SAGGRGIAVV FNDAAYGAEV NLYGLKGLAT
EPMLIDEIDF AALATAAGGQ GVVVRSLADL EVLKEWAATP VDERRFLVLD LRISGGVIAP
YQEEVIRINA
//
