ID A0A3A8AUN7_9RHOB Unreviewed; 588 AA.
AC A0A3A8AUN7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Thiamine pyrophosphate-requiring protein {ECO:0000313|EMBL:RKF12619.1};
GN ORFNames=D6850_16790 {ECO:0000313|EMBL:RKF12619.1};
OS Roseovarius spongiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=2320272 {ECO:0000313|EMBL:RKF12619.1, ECO:0000313|Proteomes:UP000281128};
RN [1] {ECO:0000313|EMBL:RKF12619.1, ECO:0000313|Proteomes:UP000281128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HN-E21 {ECO:0000313|EMBL:RKF12619.1,
RC ECO:0000313|Proteomes:UP000281128};
RA Zhuang L., Luo L.;
RT "Roseovarius spongiae sp. nov., isolated from a marine sponge.";
RL Submitted (SEP-2018) 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:RKF12619.1}.
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DR EMBL; RAPE01000006; RKF12619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A8AUN7; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000281128; 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; 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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000281128};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..542
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 588 AA; 63507 MW; 20CEA57D3F97E7D6 CRC64;
MADTVGDFIL KRLHEWGVRR IYGYPGDGIN GLVGALGRDD TIDFVQTRHE EEAAFMACAH
AKWTGEVGVC MATSGPGAIH LLNGLYDAKL DHQPVLAIVG QQARAALGGN YQQEVDLQVL
FKDVAKDYVH TCMAPAQARH LIDRGMRIAM AKRLPTALIF PNDVQEADAV EEPAHAHGTV
HSGVGFAAPR VVPEQADLTR AAEVLNAGKK VAILAGAGAL NAAEELTQAA DLLGAGVAKA
LLGKAVLPDD LPFVTGQMGL LGTEPSDWMM QHCDTLLMIG SRFPYSEFLP KEGRARAVQI
DIDPAMESIR YPMEVNLVGD AAATLRALIP HLKARGDSRW REDIEKRVAK WWDGAEDRAH
QKADPINPER LFWEASPRLP DNTIIAADSG TAANWFARAI KVRTGMKASL SGTLATMCPG
VPYATAAKFC FPERAAVGFV GDGAMQMLGI NGLITISKYW REWADPRLVI AVLNNHDLNQ
VTWELRAMGD SPKVPETQDV PPFNYADFAA SLGLNGIRVE SPDQIAPAWD EAFAADRPTV
IDARTDPDVP TLPPHISMSQ AKSYAKALAA GDPDAGGILW QTFKRVTG
//
