(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BIY9_GEOS0

ID   A0A0F6BIY9_GEOS0        Unreviewed;       390 AA.
AC   A0A0F6BIY9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 22.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   OrderedLocusNames=GY4MC1_0558 {ECO:0000313|EMBL:ADP73390.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73390.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73390.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73390.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) 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; CP002293; ADP73390.1; -; Genomic_DNA.
DR   RefSeq; WP_013400087.1; NC_014650.1.
DR   EnsemblBacteria; ADP73390; ADP73390; GY4MC1_0558.
DR   GeneID; 29236788; -.
DR   KEGG; gmc:GY4MC1_0558; -.
DR   KO; K10907; -.
DR   OMA; FYLYADV; -.
DR   OrthoDB; 554560at2; -.
DR   BioCyc; GSP581103:G1GOQ-607-MONOMER; -.
DR   Proteomes; UP000002034; 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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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; A0A0F6BIY9.
DR   SWISS-2DPAGE; A0A0F6BIY9.
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:ADP73390.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Transferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:ADP73390.1}.
FT   DOMAIN       35    383       Aminotran_1_2. {ECO:0000259|Pfam:
FT                                PF00155}.
SQ   SEQUENCE   390 AA;  43063 MW;  F4295FCBF84B1097 CRC64;
     MMQQTKKSYV SETVARLKPS GIRRFFDLAS SMEGVVSLGV GEPDFVTSWS IREASILSLE
     QGYTSYTANA GLLELRQEIA AYLARKFHVE YDPEAEILVT VGASQAIDLA LRATVNPGDE
     VIVVEPSFVS YGPLVTLAGG VPVPVGTTGE DHFKLRPDQI ERVITDRTKA LIVCSPNNPT
     GTVLHKEDLE AIAQIVKKHD LLVISDEIYA ELTYDEPYIS FAAVDGMRER TILVSGFSKG
     FAMTGWRLGF TAAPAEILQA MLKIHQYAIM CAPTMAQYAA IEALRNGEQD VEYMKKSYRR
     RRNYFVQSLN EIGLSCHMPG GAFYAFPSIR ATGLTSEQFA EKLLLEEKVA VVPGSVFGAG
     GEGYIRCSYA SSMEQLQEAI KRIKRFLERL
//

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