(data stored in SCRATCH zone)

SWISSPROT: C3MFT6_SINFN

ID   C3MFT6_SINFN            Unreviewed;       388 AA.
AC   C3MFT6;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 53.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   OrderedLocusNames=NGR_c01870 {ECO:0000313|EMBL:ACP23987.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23987.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23987.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
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
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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DR   EMBL; CP001389; ACP23987.1; -; Genomic_DNA.
DR   RefSeq; WP_012706772.1; NC_012587.1.
DR   RefSeq; YP_002824740.1; NC_012587.1.
DR   ProteinModelPortal; C3MFT6; -.
DR   STRING; 394.NGR_c01870; -.
DR   EnsemblBacteria; ACP23987; ACP23987; NGR_c01870.
DR   GeneID; 7790765; -.
DR   KEGG; rhi:NGR_c01870; -.
DR   PATRIC; fig|394.7.peg.2982; -.
DR   eggNOG; ENOG4105CHM; Bacteria.
DR   eggNOG; COG0436; LUCA.
DR   HOGENOM; HOG000223062; -.
DR   OMA; GWLRWCF; -.
DR   OrthoDB; POG091H00QO; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3MFT6.
DR   SWISS-2DPAGE; C3MFT6.
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:ACP23987.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Transferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:ACP23987.1}.
FT   DOMAIN       40    381       Aminotran_1_2. {ECO:0000259|Pfam:
FT                                PF00155}.
SQ   SEQUENCE   388 AA;  42488 MW;  A8E19FCCC2A0E7EF CRC64;
     MTIMTSLSPR ALSAPESGIV EVVNYARGRD GLIPLWVGEG DLPTPDFISR AAAQGLMGGE
     TFYTWQRGIP PLREALVRYY QRRFQKTLAP ENFYVTGSGM QAIKLSIEAI ASPGDEIVLL
     TPAWPNFAAA ADLSGVRPVS VPLRFENGKW QLDLDRLEAA IGKKTRALFI NTPSNPTGWT
     ATQDDLKAIL SLARKHGLWI IADEIYALYY YLGGRAPSFL DIMAEDDRIL FVNSFSKNWA
     MTGWRVGWIV APPAVGQVLE NLIQYSTSGV AQFMQRGAVV ALDEGDGFVD DNVAKARRNR
     DMLCDALIAT NRVETLKPDG ALYAFLKIDG VTDARRASMD IVDETGVGLA PGTAFGEGGS
     LFMRACFLRD PAQIAEAADR LRTYILGR
//

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