(data stored in ACNUC7421 zone)

SWISSPROT: Q2IND1_ANADE

ID   Q2IND1_ANADE            Unreviewed;       400 AA.
AC   Q2IND1;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 74.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   OrderedLocusNames=Adeh_0533 {ECO:0000313|EMBL:ABC80309.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC80309.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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; CP000251; ABC80309.1; -; Genomic_DNA.
DR   RefSeq; WP_011419592.1; NC_007760.1.
DR   STRING; 290397.Adeh_0533; -.
DR   EnsemblBacteria; ABC80309; ABC80309; Adeh_0533.
DR   KEGG; ade:Adeh_0533; -.
DR   eggNOG; ENOG4105CHM; Bacteria.
DR   eggNOG; COG0436; LUCA.
DR   HOGENOM; HOG000223055; -.
DR   KO; K11358; -.
DR   OMA; SQGANQY; -.
DR   BioCyc; ADEH290397:G1G5W-546-MONOMER; -.
DR   Proteomes; UP000001935; 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; Q2IND1.
DR   SWISS-2DPAGE; Q2IND1.
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:ABC80309.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW   Transferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:ABC80309.1}.
FT   DOMAIN       36    387       Aminotran_1_2. {ECO:0000259|Pfam:
FT                                PF00155}.
SQ   SEQUENCE   400 AA;  42737 MW;  75B0DEA6937142F3 CRC64;
     MDVVTRQIRS EMEGASWIRR MFDAGLELKQ RIGADNVFDF SLGNPDVPPP AAAAAALRGL
     AEQVTAPMGL GYCPNAGLPS VRAALARRLA AEQQAPVEAR HLVLTCGAAG GLVTFFRAVL
     EPGDEVLCFA PYFVEYGAYA GHFGGVLRAV PSKVPDFTPD LAALEAAIGP RTRVVLVNSP
     NNPTGRIYDA ATMRAMGALL SRVNVERGRE RPVFLVSDEP YRRLAYGGAE VAPILPLTPF
     SLVVGSFSKS LSLAGERVGY LLVNPGMPDA QVLVDALTLT NRTLGFVNAP VVGQRLVEAL
     VDESVDVAIY DRRRRAMAEA LTGAGIAFHL PEGAFYFFPE APGGDDQAFV KLLLEENILA
     VPGRGFGMPG YVRLTFCVDE QVIRRAAPGF ARAARRARGG
//

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