ID E6M322_9ACTO Unreviewed; 693 AA.
AC E6M322;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=tkt {ECO:0000313|EMBL:EFU82358.1};
GN ORFNames=HMPREF0576_0727 {ECO:0000313|EMBL:EFU82358.1};
OS Mobiluncus holmesii ATCC 35242.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Mobiluncus.
OX NCBI_TaxID=887899 {ECO:0000313|EMBL:EFU82358.1, ECO:0000313|Proteomes:UP000003343};
RN [1] {ECO:0000313|EMBL:EFU82358.1, ECO:0000313|Proteomes:UP000003343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35242 {ECO:0000313|EMBL:EFU82358.1,
RC ECO:0000313|Proteomes:UP000003343};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001027};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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:EFU82358.1}.
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DR EMBL; AEPZ01000005; EFU82358.1; -; Genomic_DNA.
DR RefSeq; WP_004010714.1; NZ_GL622346.1.
DR AlphaFoldDB; E6M322; -.
DR HOGENOM; CLU_009227_0_0_11; -.
DR Proteomes; UP000003343; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005478; Transketolase_bac-like.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00232; tktlase_bact; 1.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFU82358.1}.
FT DOMAIN 368..548
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 693 AA; 74422 MW; AC5F9F6E96118355 CRC64;
MSFVASELDK QAIKAAKALA ADAVENAGNG HPGTPISLAP AAYLLYQYVM RSDPADPWWL
GRDRFVLSAG HASALQYVQL FLAGYGIELE DLKRFRQSGG LLTGHPEYRH QPGVEVTTGP
LGTGIAAAVG MAMEQRRLRG LLDPDAAPGE SPFDHHIYVV SGDGCLQEGI SYEAMSLAGT
QELGNLIYLY DENRISIEDD IEIAFTEDIR ARFESQGWHY QEVSWLQDDG SYVENLEALF
AAFETAKAET RKPSIIKLRT IIGWPSPNKQ NQGGIHGSAL GASELEGLKT ALGLDPTKMF
DIPAEIVAAT RENVAKRAQA FRSEWDPRFA TWQQSHPQQA ALLKRLQDGK LPADVESALP
QFEPGSAIAT RAASGKVINA LAGVLPELWG GSADLAGSNN TAIADESSFA PADRATKAWT
NVSEWGRNLH FGVREHAMAG ILNGIATSGL TRPYAGTFLV FSDFMRGAVR LSALMKLPVT
YVWTHDSIGV GEDGPTHQPV ETLTSLRAIP NLAVVRPADG AETAYAWLEI MRRRGPAGLA
LSRQKLPNPA RGADTGLASA KNVARGGYVL KDFGDNPAVI LLATGSEVAL ALQAGEKLAE
EGVVARVVSL PCLEWFEEQD AAYRESVLPT SIRARVSIEA GLAMPWYRYL GDAGTAVSVE
TFGTPASGAD NFAHFGFTVE NVVAKAKESL VKA
//
