ID K2I5R4_9RHOB Unreviewed; 542 AA.
AC K2I5R4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Thiamine pyrophosphate protein {ECO:0000313|EMBL:EKE44300.1};
GN ORFNames=OCGS_1816 {ECO:0000313|EMBL:EKE44300.1};
OS Oceaniovalibus guishaninsula JLT2003.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Oceaniovalibus.
OX NCBI_TaxID=1231392 {ECO:0000313|EMBL:EKE44300.1, ECO:0000313|Proteomes:UP000006765};
RN [1] {ECO:0000313|EMBL:EKE44300.1, ECO:0000313|Proteomes:UP000006765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT2003 {ECO:0000313|EMBL:EKE44300.1,
RC ECO:0000313|Proteomes:UP000006765};
RX PubMed=23144420; DOI=10.1128/JB.01874-12;
RA Tang K., Liu K., Jiao N.;
RT "Draft Genome Sequence of Oceaniovalibus guishaninsula JLT2003T.";
RL J. Bacteriol. 194:6683-6683(2012).
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:EKE44300.1}.
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DR EMBL; AMGO01000036; EKE44300.1; -; Genomic_DNA.
DR RefSeq; WP_007426968.1; NZ_AMGO01000036.1.
DR AlphaFoldDB; K2I5R4; -.
DR STRING; 1231392.OCGS_1816; -.
DR PATRIC; fig|1231392.3.peg.1826; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000006765; 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:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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 Reference proteome {ECO:0000313|Proteomes:UP000006765};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 376..521
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 542 AA; 56977 MW; 539D7A95D56F1D20 CRC64;
MRHGGEILVA ALKAQGVDRV FSVPGESFLA ALDGLHGSGI RNVVCRHEGG AAMMAEADGK
LTGRPGVVMV TRGPGACNAS SGLHVARQDS TPLVCFVGQI ARAHRDREAF QEVDYRAMFG
PLVKWAAEVD QTERLPEYVM RAFHIATSGR PGPVVLALPE DMLSAQADTP DLAATAPVSG
GVTDAMLSAI EARLDAARRP LVVLGGSDWS QEAAEGIRAF AEGRGLPVAV SFRRQGHIDN
RSPCYAGDLG VGMNPALGAT LAASDCLLVL GARLGDIASG GYRHIDPAAP PPIVHIHPDP
DEIGKVFRAD LGIVARAAEV AVALGRRAAP PAAAPVARAD YEAWQDPRPT SGRVRMEDVV
TWLSANLPED AIVTNGAGNY AAWLHRYFRF KRYGTQLAPT SGSMGYGFPA AIAASLRHPG
CAVVCLAGDG CFQMTLNEMS TAVQHGAAPV VIVCNNGRYG TIRVHQERAY PGRVSGTDLA
NPDFAALARA YGGHGEIVED NADLAAAFDR ARRSGTVAVI ELRLDPDVLS PTLSLTGMQT
AR
//