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Database: UniProt
Entry: H6NME3_9BACL
LinkDB: H6NME3_9BACL
Original site: H6NME3_9BACL 
ID   H6NME3_9BACL            Unreviewed;       326 AA.
AC   H6NME3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=BfmBAB {ECO:0000313|EMBL:AFC29809.1};
GN   ORFNames=PM3016_2939 {ECO:0000313|EMBL:AFC29809.1};
OS   Paenibacillus mucilaginosus 3016.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1116391 {ECO:0000313|EMBL:AFC29809.1, ECO:0000313|Proteomes:UP000007523};
RN   [1] {ECO:0000313|EMBL:AFC29809.1, ECO:0000313|Proteomes:UP000007523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3016 {ECO:0000313|EMBL:AFC29809.1,
RC   ECO:0000313|Proteomes:UP000007523};
RX   PubMed=22535950; DOI=10.1128/JB.00323-12;
RA   Ma M., Wang Z., Li L., Jiang X., Guan D., Cao F., Chen H., Wang X.,
RA   Shen D., Du B., Li J.;
RT   "Complete Genome Sequence of Paenibacillus mucilaginosus 3016, a Bacterium
RT   Functional as Microbial Fertilizer.";
RL   J. Bacteriol. 194:2777-2778(2012).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP003235; AFC29809.1; -; Genomic_DNA.
DR   RefSeq; WP_013916417.1; NC_016935.1.
DR   AlphaFoldDB; H6NME3; -.
DR   STRING; 1116391.PM3016_2939; -.
DR   KEGG; pmq:PM3016_2939; -.
DR   HOGENOM; CLU_012907_1_0_9; -.
DR   Proteomes; UP000007523; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000007523}.
FT   DOMAIN          4..178
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   326 AA;  35223 MW;  06DFFB9768F1C865 CRC64;
     MAVITYLEAI RTAMKEEMER DESVFVLGED VGKGGVMNAT KGLRDQFGEE RVMDTPLAES
     AIAGVAIGAA MYGMKPIAEM QYADFIFPAT NQIISEAALI RYRSNNDWNC PVVVRAPYGA
     TGGGALYHSQ CPESVFFGIP GLKIVAPSNP YDAKGLLKAA VRDADPVLYF EHKKCYLGIT
     GEVPEEDYIV PIGKADVKRE GTDITVISYG ITVQYALRAA EELAAEGISA HVLDLRTLQP
     LDKEAILAAA SKTGKVLIVH EDNKTGGVGA EVSALIAEEL LFELDAPIMR LCGPDVPAVG
     MNPPMEKFFL LSTDKIMEAM RKLALF
//
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