ID L8TRQ8_9MICC Unreviewed; 564 AA.
AC L8TRQ8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Thiamine pyrophosphate-dependent enzyme, carboligase or decarboxylase {ECO:0000313|EMBL:ELT45417.1};
GN ORFNames=G205_05136 {ECO:0000313|EMBL:ELT45417.1};
OS Arthrobacter nitrophenolicus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=683150 {ECO:0000313|EMBL:ELT45417.1, ECO:0000313|Proteomes:UP000011189};
RN [1] {ECO:0000313|Proteomes:UP000011189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJCon {ECO:0000313|Proteomes:UP000011189};
RX PubMed=23516196; DOI=10.1128/genomeA.00058-13;
RA Vikram S., Kumar S., Vaidya B., Pinnaka A.K., Raghava G.P.;
RT "Draft Genome Sequence of the 2-Chloro-4-Nitrophenol-Degrading Bacterium
RT Arthrobacter sp. Strain SJCon.";
RL Genome Announc. 1:e0005813-e0005813(2013).
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:ELT45417.1}.
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DR EMBL; AOFD01000008; ELT45417.1; -; Genomic_DNA.
DR RefSeq; WP_009356915.1; NZ_AOFD01000008.1.
DR AlphaFoldDB; L8TRQ8; -.
DR PATRIC; fig|683150.5.peg.1032; -.
DR Proteomes; UP000011189; Unassembled WGS sequence.
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; 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:SF167; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVB2-RELATED; 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 Ligase {ECO:0000313|EMBL:ELT45417.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011189};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 19..137
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 209..340
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 407..550
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 564 AA; 59674 MW; CDFA79168413CE55 CRC64;
MIDFDPGTTA PTKGTGARNG GDLVVETLEA LGAKTVFGIP GQHALGLFDA MGRGNLQFVS
SRVENNSAFA ADGYSRATGE VGVLFLSTGP GALTSLAGLQ EAYATGVPMV VVASQIPLEG
LGARRKGMLH QLDDQKASAA NVTKSQRLIQ HASGIPSAIQ DAWTEAISSP QGPVWIEIPQ
NVLLDPIMVP PVEDALAEAA DNPPRVELVR EAVKWLEAAE RPAIIAGGGT RRGRAEKSLL
SIAEKLRAPV ICTPGGNGAF PWNHELSLQS WIEDRHMTDL LEDADVLVVI GSSLGEVTSN
YFTFEPRGRI IQIDAEPRVL ESNRPGLGIR ADAGQALAAL DEALSPERAV EPGWHGVPPE
ELVKESLAKV KARLESQDLG KELKFMADIR EAVPADMQTF WDMTIAAYWA WSCWDAREGQ
FHSAQGAGGL GYGFPAAIGA AVGLETLGKP GRVLAVSGDG SSMYSISELA TARQHNVPVT
WLIVDDGGYG ILREYMVGAF GKATATELAR PDFVKLAEAF GVPAIRVAPE DVGDALRAGF
AADGPNVVVV ETLLKMFAPT HLDG
//