ID H5YGE2_9BRAD Unreviewed; 595 AA.
AC H5YGE2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Thiamine pyrophosphate-dependent enzyme, possible carboligase or decarboxylase {ECO:0000313|EMBL:EHR01741.1};
GN ORFNames=Bra471DRAFT_02481 {ECO:0000313|EMBL:EHR01741.1};
OS Bradyrhizobium sp. WSM471.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=319017 {ECO:0000313|EMBL:EHR01741.1};
RN [1] {ECO:0000313|EMBL:EHR01741.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM471 {ECO:0000313|EMBL:EHR01741.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA Howieson J., Reeve W., Woyke T.;
RT "The Noncontiguous Finished sequence of Bradyrhizobium sp. WSM471.";
RL Submitted (NOV-2011) 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; CM001442; EHR01741.1; -; Genomic_DNA.
DR RefSeq; WP_007607333.1; NZ_CM001442.1.
DR AlphaFoldDB; H5YGE2; -.
DR HOGENOM; CLU_013748_3_0_5; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000005774; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 Ligase {ECO:0000313|EMBL:EHR01741.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 595 AA; 64435 MW; E88525576D672F23 CRC64;
MSQTVSDFIV QRLHQWGVRH LFGYPGDGIN GVFGALQRAE GKIGFVQTRH EEMAAFMATA
YAKFSGQLGV CIATSGPGAS HLITGLYDAL LDHQPVLAIV GQQARNALGG HYQQELDLVS
MFKDVAGAYV MQASSPAQIR HLIDRSIRIA LARRTPTVVI LPNDIQEEPY EDPPRAHGTL
HSGVGYSAPS IKPRDTDLDR AAEVLNAGKK VAMLIGAGAL HATEEVIAVA DRLSAGCAKA
LLGKAALPDD LPWVTGSIGL LGTEPSYNMM MECDTLLMVG SGFPYSEFLP KEGAARGVQI
DIDASMMSIR FPMEVGLVGD AAETLRALLP RLAPKTDGAW RQGIQEDVAK WWKTLDDRAH
QPAAPVNPQL VTWELSPRLP DRAIITSDSG SCANWFARDL KMRRGMTASL SGGLASMGAA
VPYALAAKYA HSDRPVIALV GDGAMQMNNM AELITAAKYW RDWKDPRFVV CVFNNEDLNQ
VTWEQRIING DPKFEASQRI PNVSYSRFAE LIGLSGIYVD SPQMLGSAWE QALASRMPVV
LEVKTDPEVP PLPPHITLQQ AKNFALALMK GDPNESGVIK GAARQVLEKI LPGSE
//
