(data stored in SCRATCH zone)

SWISSPROT: C8VVD5_DESAS

ID   C8VVD5_DESAS            Unreviewed;       402 AA.
AC   C8VVD5;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 53.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   OrderedLocusNames=Dtox_0041 {ECO:0000313|EMBL:ACV61005.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61005.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61005.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(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; CP001720; ACV61005.1; -; Genomic_DNA.
DR   STRING; 485916.Dtox_0041; -.
DR   EnsemblBacteria; ACV61005; ACV61005; Dtox_0041.
DR   KEGG; dae:Dtox_0041; -.
DR   eggNOG; ENOG4105CHM; Bacteria.
DR   eggNOG; COG0436; LUCA.
DR   HOGENOM; HOG000223062; -.
DR   KO; K10907; -.
DR   OMA; FYLYADV; -.
DR   BioCyc; DACE485916:G1GFV-45-MONOMER; -.
DR   Proteomes; UP000002217; 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; C8VVD5.
DR   SWISS-2DPAGE; C8VVD5.
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:ACV61005.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Transferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:ACV61005.1}.
FT   DOMAIN       43    392       Aminotran_1_2. {ECO:0000259|Pfam:
FT                                PF00155}.
SQ   SEQUENCE   402 AA;  44695 MW;  4279ECB396FC00FC CRC64;
     MSEVVKMEER KGSPDWSEFI NPVLKSLPPS GIRRFFDLVS EMKDVVSLGV GEPDFVTPRN
     IIDACVRSLD NGQTGYTSNQ GMLELREAIA EEINGSYGVK YDPVSEILIT VGVSEALDLA
     MRALISPGDE VLIPEPTYVS YIPCAALAYA KTVPLKTNMD KLFRVTAEQV EKAITPRTKI
     LLLAYPNNPT GAVMTRQELL DICEVVKAHN LIVISDEIYE HLTYIEPHTC VSSLPGMKER
     TILLSGFSKS YAMTGWRAGY ACGNPDFIGA MTKIHQYSML CAPTQAQVCA LEALRSGKPD
     MRRMTAEYNK RRKLVVDAME EIGLPCFEPG GAFYAFPDIT KTRMNAAEFS ERLLMEEKVA
     VVDGTAFGEA GEGHVRISYA YSVEKLTEAF RRMNRFVKRY SS
//

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