ID A0A0P7VW62_9RHOB Unreviewed; 542 AA.
AC A0A0P7VW62;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Thiamine pyrophosphate-requiring enzyme {ECO:0000313|EMBL:KPP87516.1};
GN ORFNames=HLUCCO07_10740 {ECO:0000313|EMBL:KPP87516.1};
OS Rhodobacteraceae bacterium HLUCCO07.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666914 {ECO:0000313|EMBL:KPP87516.1, ECO:0000313|Proteomes:UP000050369};
RN [1] {ECO:0000313|EMBL:KPP87516.1, ECO:0000313|Proteomes:UP000050369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCO07 {ECO:0000313|EMBL:KPP87516.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) 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:KPP87516.1}.
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DR EMBL; LJSU01000010; KPP87516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7VW62; -.
DR STRING; 1666914.HLUCCO07_10740; -.
DR PATRIC; fig|1666914.4.peg.129; -.
DR Proteomes; UP000050369; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 191..320
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 392..529
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 542 AA; 58815 MW; 1A0F2AD521C99057 CRC64;
MSESKDYTYQ SIARSVLDQG VDTMFGLMGD ANLFMVDHFV RHCGGTFVPV AYEGSSVLMA
LAYSHVAGRV GVATVTHGPA LTNCTTALAE GARGHVPMVL LAGDTPVMNP QHLQSIDQRE
LVKVTGAGFE QMRAPETASY DIAHAFYRAK IEKRPIVLNM PADFMWLETV HEKKVFQVFE
TPAYVPEGDG VDQAIGMIAS ARRPVILAGA GATGARDSLI RLADRLQAPL ATTLKAKGLF
NDHPYNMDIF GTLSTPAAYE VIDKADCVVA FGASLHAFTT DQGKLMKGKR VIQINEDPAQ
ISFNYHPDAA LAADARLTAE NIIYWLDEAE IAPSGFTEEL DRETLTAHPP GQAEKAKPGY
VNYVYALDRL EEALPKDRIL TTDGGRFMTE VWCRISAPDP KSFIATTNFG SIGIGLQEAI
GASIAAPDRP VVLFTGDGGF MMGGVNEFNT AVRLKQDLIV ILCNDSAYGA EHIQFLDKRM
DPGLSQFDWP CFAEVATALG GQGVYVQSAE ELDAAIEAIE SRDGPLLIEL RLDPHDVPRM
RI
//