(data stored in ACNUC7421 zone)

SWISSPROT: D6XV64_BACIE

ID   D6XV64_BACIE            Unreviewed;       286 AA.
AC   D6XV64;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 57.
DE   SubName: Full=Aminotransferase class IV {ECO:0000313|EMBL:ADH97622.1};
GN   OrderedLocusNames=Bsel_0072 {ECO:0000313|EMBL:ADH97622.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97622.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97622.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU004516};
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU004106}.
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DR   EMBL; CP001791; ADH97622.1; -; Genomic_DNA.
DR   RefSeq; WP_013171052.1; NC_014219.1.
DR   STRING; 439292.Bsel_0072; -.
DR   EnsemblBacteria; ADH97622; ADH97622; Bsel_0072.
DR   KEGG; bse:Bsel_0072; -.
DR   eggNOG; ENOG4107W20; Bacteria.
DR   eggNOG; COG0115; LUCA.
DR   HOGENOM; HOG000276706; -.
DR   KO; K02619; -.
DR   OMA; VNTTNAC; -.
DR   OrthoDB; 1275805at2; -.
DR   BioCyc; BSEL439292:G1GLR-79-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR018300; Aminotrans_IV_CS.
DR   InterPro; IPR036038; Aminotransferase-like.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   SUPFAM; SSF56752; SSF56752; 1.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XV64.
DR   SWISS-2DPAGE; D6XV64.
KW   Aminotransferase {ECO:0000313|EMBL:ADH97622.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU004516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Transferase {ECO:0000313|EMBL:ADH97622.1}.
SQ   SEQUENCE   286 AA;  32027 MW;  7C14EC0E85CC7218 CRC64;
     MYIKVNGTII PEEEARISPL DHGFLYGMGL FETFRTYDGH PFLLDEHMKR LREGADEMNI
     QLPAYDRQDV VETIRALLAA NKNRDLYFRW NVTAGHGGVG LTAEPYEEPG ELVFVKDAPT
     PPATKQARVL TQTRNTPEGA VRRKSHHYMN SMLAKQELGQ DPGTEGMMLT SDGHVSEGIV
     SNVFWVKKDT LYTPSLETGC LPGVTRAWVA DYADKQRLPF QEGFFTAADM MQAEAVFVTN
     AIQEIVPVTA IDGRPFDSQT NPHLLALKQQ YEIDKKQAYS LGECGL
//

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