ID   C1BBR5_RHOOB            Unreviewed;       388 AA.
AC   C1BBR5;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   OrderedLocusNames=ROP_48710 {ECO:0000313|EMBL:BAH53118.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH53118.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH53118.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH53118.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         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; AP011115; BAH53118.1; -; Genomic_DNA.
DR   RefSeq; WP_015888630.1; NC_012522.1.
DR   AlphaFoldDB; C1BBR5; -.
DR   STRING; 632772.ROP_48710; -.
DR   KEGG; rop:ROP_48710; -.
DR   PATRIC; fig|632772.20.peg.5091; -.
DR   HOGENOM; CLU_017584_4_3_11; -.
DR   OrthoDB; 9763453at2; -.
DR   Proteomes; UP000002212; 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   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR46383:SF2; (5-FORMYLFURAN-3-YL)METHYL PHOSPHATE TRANSAMINASE; 1.
DR   PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:BAH53118.1};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:BAH53118.1}.
FT   DOMAIN          31..382
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   388 AA;  41522 MW;  A53AEEFD6CA3E39E CRC64;
     MRPESQRSNI QTFHVMDVWK AATERQRTHG DVLTLAAGQP STPAPQPVLR ATREVLDGHL
     LGYTETFGIL PLREAIAGYH AGKSGIDVDA EDVVVTTGSS GAFTLLFLAA FDVGDTVVVA
     RPGYPAYRNT LAALGCTVIE IDCGADTRFQ PTVAMLDALP EPPAGLIVAS PANPTGTVID
     PGELAALARW CDAHGTLLIS DEIYHGIGYG EQAMTSSWET SRESVVVGSV SKYFSMTGWR
     LGWMLVPEGL RRPLQRLASN MTVCPPAISQ HAAIAAFTEE SRAELDGHVQ RYAVNRELLL
     TGLPELGITD LAPADGAFYV YADIGHLLGG SHGATSTEWC SRLLQDTGLA LAPGIDFDTV
     HGDRTVRLSF AGSTAEVRES LVRLGRWL
//