ID   YTET_BACSU              Reviewed;         428 AA.
AC   O34371; Q795R6;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Putative oxidoreductase YteT;
DE            EC=1.-.-.-;
DE   Flags: Precursor;
GN   Name=yteT; OrderedLocusNames=BSU30100;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT   200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   INDUCTION, AND FUNCTION.
RC   STRAIN=168;
RX   PubMed=17449691; DOI=10.1128/aem.00147-07;
RA   Ochiai A., Itoh T., Kawamata A., Hashimoto W., Murata K.;
RT   "Plant cell wall degradation by saprophytic Bacillus subtilis strains: gene
RT   clusters responsible for rhamnogalacturonan depolymerization.";
RL   Appl. Environ. Microbiol. 73:3803-3813(2007).
CC   -!- FUNCTION: May play a role in the degradation of type I
CC       rhamnogalacturonan derived from plant cell walls.
CC       {ECO:0000269|PubMed:17449691}.
CC   -!- INDUCTION: Up-regulated by growth on type I rhamnogalacturonan.
CC       {ECO:0000269|PubMed:17449691}.
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR   EMBL; AF008220; AAC00274.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14988.1; -; Genomic_DNA.
DR   PIR; C69991; C69991.
DR   RefSeq; NP_390888.1; NC_000964.3.
DR   RefSeq; WP_009968003.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34371; -.
DR   SMR; O34371; -.
DR   STRING; 224308.BSU30100; -.
DR   PaxDb; O34371; -.
DR   DNASU; 937274; -.
DR   EnsemblBacteria; CAB14988; CAB14988; BSU_30100.
DR   GeneID; 937274; -.
DR   KEGG; bsu:BSU30100; -.
DR   PATRIC; fig|224308.179.peg.3267; -.
DR   eggNOG; COG0673; Bacteria.
DR   InParanoid; O34371; -.
DR   OMA; YFKRWNR; -.
DR   PhylomeDB; O34371; -.
DR   BioCyc; BSUB:BSU30100-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   Oxidoreductase; Reference proteome; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..428
FT                   /note="Putative oxidoreductase YteT"
FT                   /id="PRO_0000378077"
SQ   SEQUENCE   428 AA;  48892 MW;  ABF2ABA8E85D6F43 CRC64;
     MKNIVFCGLS SRAFSMFIKP LMERFSTHYE ITGLLDADPK RFAVCKKKFP ELAHVPEFSE
     DAFDEMMRVS KPDIVIVAGR DDTHVAYIVK SLQWNTDVIT EKPMVTTVQD ANRVLEAEAK
     SEGKVTVAFN YRYSPFHRKI KEMILDGKIG RVTSVDLNWY IDTYHGASYF KRWNRSRQFS
     GGLSVHKSTH HFDLVNWWLG QNPEEVFAYG ALNYYGPDSE WNPLPEEDGR FCGTCRVKEK
     CHYYSRWHPR SSKASIKDDH LEAGDQSSLY TAYRPDACIF DEEIDIEDTY VAAVKYDGGA
     LLSYSIIFSA PYEGYRLTIN GTKGRIESNE FHEPSRIPFA FPEQTIEYYP LFESKQTIQV
     VKNEGGHGGG DPLLLEDLFL GKDPLRRYDI LAGAEAGAYS IAVGEGMWRS VAEKKPIGMK
     ELFQMQNV