ID   Y4MN_SINFN              Reviewed;         345 AA.
AC   P55573;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=Putative uncharacterized transketolase family protein y4mN;
GN   OrderedLocusNames=NGR_a02450; ORFNames=y4mN;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234a.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=9163424; DOI=10.1038/387394a0;
RA   Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA   Perret X.;
RT   "Molecular basis of symbiosis between Rhizobium and legumes.";
RL   Nature 387:394-401(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. Corresponds to the C-
CC       terminal of members of this family. {ECO:0000305}.
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DR   EMBL; U00090; AAB91777.1; -; Genomic_DNA.
DR   RefSeq; NP_443980.1; NC_000914.2.
DR   RefSeq; WP_010875270.1; NC_000914.2.
DR   AlphaFoldDB; P55573; -.
DR   SMR; P55573; -.
DR   KEGG; rhi:NGR_a02450; -.
DR   PATRIC; fig|394.7.peg.255; -.
DR   eggNOG; COG3958; Bacteria.
DR   HOGENOM; CLU_009227_1_1_5; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000001054; Plasmid sym pNGR234a.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd07033; TPP_PYR_DXS_TK_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; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   PANTHER; PTHR43825:SF1; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN; 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   5: Uncertain;
KW   Plasmid; Reference proteome; Thiamine pyrophosphate.
FT   CHAIN           1..345
FT                   /note="Putative uncharacterized transketolase family
FT                   protein y4mN"
FT                   /id="PRO_0000191912"
SQ   SEQUENCE   345 AA;  37509 MW;  E6711A19D2D4253D CRC64;
     MRRSKYERPA HLIGNAERPR LTTSAMIASI AGADQPTRPA PFGHALSALA EKDDRVVGLS
     ADLAKYTDLH VFRAAHPDRF YQMGMAEQLL MMSAAGMARE GLQPWVTTYA VFASRRAYDF
     ICLAIAEEML DVKVVCALPG LTTGYGPSHQ ATEDIAMFRG MPNLTIIDPC DASEIEQAVP
     AIAAHEGPVY MRLLRGNVPL VLEEYGYRFE LGKAKLLRDG RDTLIISSGL MTMRALEAAE
     ELRKNGIDAG VLHVPTIKPL DEATILAECA RQGRLVVVAE NHTVIGGLGE AVAATLMRSA
     VRPAAFRQIG LPDAFLEAGA LPTLHDMYGI STTKIVAQIK EWLDE
//