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Database: UniProt
Entry: A0A024H514_9MICC
LinkDB: A0A024H514_9MICC
Original site: A0A024H514_9MICC 
ID   A0A024H514_9MICC        Unreviewed;       336 AA.
AC   A0A024H514;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Transketolase, C-terminal domain protein {ECO:0000313|EMBL:CCQ46831.1};
DE            EC=1.2.4.1 {ECO:0000313|EMBL:CCQ46831.1};
GN   Name=pdhB2 {ECO:0000313|EMBL:CCQ46831.1};
GN   ORFNames=ARTSIC4J27_2804 {ECO:0000313|EMBL:CCQ46831.1};
OS   Pseudarthrobacter siccitolerans.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Pseudarthrobacter.
OX   NCBI_TaxID=861266 {ECO:0000313|EMBL:CCQ46831.1, ECO:0000313|Proteomes:UP000035722};
RN   [1] {ECO:0000313|Proteomes:UP000035722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4J27 {ECO:0000313|Proteomes:UP000035722};
RX   PubMed=24948757; DOI=10.1128/genomeA.00526-14;
RA   Manzanera M., Santa-Cruz-Calvo L., Vilchez J.I., Garcia-Fontana C.,
RA   Silva-Castro G.A., Calvo C., Gonzalez-Lopez J.;
RT   "Genome Sequence of Arthrobacter siccitolerans 4J27, a Xeroprotectant-
RT   Producing Desiccation-Tolerant Microorganism.";
RL   Genome Announc. Announc.2:e00526-e00514(2014).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:CCQ46831.1}.
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DR   EMBL; CAQI01000046; CCQ46831.1; -; Genomic_DNA.
DR   RefSeq; WP_050055725.1; NZ_CAQI01000046.1.
DR   AlphaFoldDB; A0A024H514; -.
DR   STRING; 861266.ARTSIC4J27_2804; -.
DR   OrthoDB; 3457658at2; -.
DR   Proteomes; UP000035722; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:CCQ46831.1}.
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   336 AA;  36404 MW;  C76D9819656DF177 CRC64;
     MTQMTFARAI NAGLRKSLEN DPKVVLLGED IGALGGVFRV TDGLQKDFGK HRVVDTPLAE
     SAIVGTAVGL AYRGYRPVVE IQFDGFIYPA FDQIVSQVAK LHYRTRGAVK MPITIRVPFG
     GGIGSPEHHS ESPEAYFTHT SGLRVVTVSN PQDAHTVIQQ AISCDDPVLY FEPKRRYHDK
     GEVDENMDPR TAVPMDRARV VTEGADVTLV AYGPLVKTAR DAASAAADEG IFIEVIDLRS
     LAPVDYDTVV ASVRKTGRLV VTHEAGQSGG LGAEVAASIT ERCFYYLEAA PVRVTGFDIP
     YPYSKLEMHH LPGLDRILDG VDRALGRPNS LSGLEG
//
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