(data stored in SCRATCH zone)

SWISSPROT: B4SR25_STRM5

ID   B4SR25_STRM5            Unreviewed;       400 AA.
AC   B4SR25;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   16-JAN-2019, entry version 58.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   OrderedLocusNames=Smal_0021 {ECO:0000313|EMBL:ACF49726.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49726.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49726.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49726.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001111; ACF49726.1; -; Genomic_DNA.
DR   RefSeq; WP_012509610.1; NC_011071.1.
DR   STRING; 391008.Smal_0021; -.
DR   EnsemblBacteria; ACF49726; ACF49726; Smal_0021.
DR   KEGG; smt:Smal_0021; -.
DR   eggNOG; ENOG4105CGF; Bacteria.
DR   eggNOG; COG1448; LUCA.
DR   HOGENOM; HOG000185899; -.
DR   KO; K00832; -.
DR   OMA; RDTNPKK; -.
DR   OrthoDB; 417859at2; -.
DR   BioCyc; SMAL391008:SMAL_RS00105-MONOMER; -.
DR   Proteomes; UP000001867; 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   GO; GO:0006520; P:cellular amino acid metabolic 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; IPR000796; Asp_trans.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR11879; PTHR11879; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00799; TRANSAMINASE.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4SR25.
DR   SWISS-2DPAGE; B4SR25.
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:ACF49726.1}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Transferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:ACF49726.1}.
FT   DOMAIN       29    394       Aminotran_1_2. {ECO:0000259|Pfam:
FT                                PF00155}.
FT   COILED      307    327       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   400 AA;  43022 MW;  99601CEDA845AB16 CRC64;
     MSFFANVELV PGDPILGLTE AYNADSRPTK VNLGVGIYYD ESGRIPLLRA VKQIEQQLAN
     EAKPRGYLPI DGLPAYTQAT RELVFGKDSP LLAAGRVTTA QTVGGSGALR VGADVLKKLL
     PHATVALSNP SWENHRAVFS AAGFEVVDYT YFDPTTHGVN FDGLLADLGK LEAGTVVLLH
     ACCHNPTGAD LTVTQWKQVA QLLKDKQLFP FIDMAYQGFD KGIEQDGAAV RIIAEAGIDS
     FIVANSYSKS FSLYGERVGA LSMVAPTAAD AKAVQSQVKR VIRTIYSSPS THGAALVAGV
     LTNPELRAMW EQELTEMRER IHALRQGLVE KLAAAGAPQF GFINEQAGMF SYSGLSREQV
     ERLRDEFGIY AVGTGRICVA ALNQNNLEYV AKAVATVAKG
//

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