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YODT_BACSU
ID   YODT_BACSU              Reviewed;         444 AA.
AC   O34662; O30468;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Uncharacterized aminotransferase YodT;
DE            EC=2.6.-.-;
GN   Name=yodT; Synonyms=yokM; OrderedLocusNames=BSU19740;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9734814; DOI=10.1093/dnares/5.3.195;
RA   Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A., Ehrlich S.D.,
RA   Park S.-H.;
RT   "Sequence analysis of the Bacillus subtilis 168 chromosome region between
RT   the sspC and odhA loci (184 degrees-180 degrees).";
RL   DNA Res. 5:195-201(1998).
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).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AF015775; AAB72074.1; -; Genomic_DNA.
DR   EMBL; AF006665; AAB81154.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13865.1; -; Genomic_DNA.
DR   PIR; F69904; F69904.
DR   RefSeq; NP_389855.1; NC_000964.3.
DR   RefSeq; WP_003230836.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34662; -.
DR   SMR; O34662; -.
DR   STRING; 224308.BSU19740; -.
DR   PaxDb; O34662; -.
DR   PRIDE; O34662; -.
DR   DNASU; 940050; -.
DR   EnsemblBacteria; CAB13865; CAB13865; BSU_19740.
DR   GeneID; 940050; -.
DR   KEGG; bsu:BSU19740; -.
DR   PATRIC; fig|224308.179.peg.2161; -.
DR   eggNOG; COG0161; Bacteria.
DR   InParanoid; O34662; -.
DR   OMA; PLVPYNA; -.
DR   PhylomeDB; O34662; -.
DR   BioCyc; BSUB:BSU19740-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..444
FT                   /note="Uncharacterized aminotransferase YodT"
FT                   /id="PRO_0000120536"
FT   MOD_RES         268
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        366..377
FT                   /note="ADQKTKKVFPPE -> QTKKRRKCFRQQ (in Ref. 1; AAB81154)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   444 AA;  48413 MW;  1B41E974A334A397 CRC64;
     MSSYLIKPEL SSAYPVVSYA KGSYVYDQTG KKYLDGSSGA VTCNIGHGVR DVTEKLKEQL
     DQVSFAYRSQ FTSEPAEQLA ALLAQELPGD VNWSFFVNSG SEAIETAMKI AIQYWQEKKQ
     TQKSIFLSRW SSYHGITLGA LSLSGFYERR YRFTHLIERY PAISAPHIYR LNHETEEDFV
     QTAADELDTM IKRIGSQFIA GFVAEPIIGA AGAAITPPPG YYERLSEVCR THDVLFIADE
     VMTGLGRTGR MLATEHWDTV PDIAVLGKGL GAGYAPIAAA VVSDSIIETI KQGSGVIMSG
     HTYSAHPYSA KAALEVLRYV LKHGLIKQSE KKGAVLKKKL DEAASQSGII GEVRGKGLLL
     GIEFVADQKT KKVFPPEQAI TQLIVSEAKK RGLIVYPSKA GIDSGEGDAV IIAPPFTISD
     GEMEELISIF SETVAAVEKN LKKD
 
 
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