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Database: UniProt
Entry: A0A102D603_9SPHN
LinkDB: A0A102D603_9SPHN
Original site: A0A102D603_9SPHN 
ID   A0A102D603_9SPHN        Unreviewed;       420 AA.
AC   A0A102D603;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   28-FEB-2018, entry version 11.
DE   SubName: Full=Aminotransferase V {ECO:0000313|EMBL:KUR75631.1};
GN   ORFNames=AQZ49_14275 {ECO:0000313|EMBL:KUR75631.1};
OS   Novosphingobium sp. FSW06-99.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1739113 {ECO:0000313|EMBL:KUR75631.1, ECO:0000313|Proteomes:UP000061032};
RN   [1] {ECO:0000313|EMBL:KUR75631.1, ECO:0000313|Proteomes:UP000061032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSW06-99 {ECO:0000313|EMBL:KUR75631.1,
RC   ECO:0000313|Proteomes:UP000061032};
RA   Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA   Glaeser S.;
RT   "Draft genome sequence of Novosphingobium sp. FSW06-99 (=LMG 27919), a
RT   Novosphingobium acidiphilum related species isolated from a surface
RT   water sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000524-50,
CC         ECO:0000256|SAAS:SAAS00607652};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|SAAS:SAAS00538721}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KUR75631.1}.
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DR   EMBL; LLZQ01000019; KUR75631.1; -; Genomic_DNA.
DR   EnsemblBacteria; KUR75631; KUR75631; AQZ49_14275.
DR   Proteomes; UP000061032; Unassembled WGS sequence.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000524; SPT; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|SAAS:SAAS00009560,
KW   ECO:0000313|EMBL:KUR75631.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000061032};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000524-50,
KW   ECO:0000256|SAAS:SAAS00009548};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061032};
KW   Transferase {ECO:0000256|SAAS:SAAS00009570,
KW   ECO:0000313|EMBL:KUR75631.1}.
FT   DOMAIN       46    361       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
FT   MOD_RES     209    209       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR000524-50}.
SQ   SEQUENCE   420 AA;  44690 MW;  02E1557C35B378D1 CRC64;
     MSKNWENAVL DPLLFGEIDP PQRLLMGPGP VNAHPRVLRA MSADLLGQFD PEMTGYMNQV
     MALYRPVFGT TNRWTMLIDG TARAAIEAGL VSLLQPGDTA LVVNFGRFGL LLQEILTRIG
     VSYETVDAPW GEVVPIEAIR AAALRTAPRV IATVHGDTST TMAQPLDGIG AIAREVGALV
     YVDATATLGG MDIATDRWGV DVVTGGLQKC LGGPSGVGPI TVSDRAADHI FSRRHDERGI
     RAAGAVDGPG ARIASNYFDL AMIMDYWSEK RLNHHTEATS MLYGARECAR IALGEGLPAR
     YARHRAAGAA MSAGLRAMGL TLFGDDAHRM TNVTGVYIPA GIDGESVRTM MREAFEIEIG
     TAFGPLVGKV WRLGAMGYNA MKHKVLLTLA ALEATLKAHG HVVPLGEAVP AALAAWEAAS
//
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