ID   A0A1M7B9J3_9RHOB        Unreviewed;       397 AA.
AC   A0A1M7B9J3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:SHL51708.1};
GN   ORFNames=SAMN05444414_11715 {ECO:0000313|EMBL:SHL51708.1};
OS   Roseovarius marisflavi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1054996 {ECO:0000313|EMBL:SHL51708.1, ECO:0000313|Proteomes:UP000184191};
RN   [1] {ECO:0000313|EMBL:SHL51708.1, ECO:0000313|Proteomes:UP000184191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29327 {ECO:0000313|EMBL:SHL51708.1,
RC   ECO:0000313|Proteomes:UP000184191};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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:RU003693};
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FRBN01000017; SHL51708.1; -; Genomic_DNA.
DR   RefSeq; WP_073198992.1; NZ_FRBN01000017.1.
DR   AlphaFoldDB; A0A1M7B9J3; -.
DR   STRING; 1054996.SAMN05444414_11715; -.
DR   OrthoDB; 9804407at2; -.
DR   Proteomes; UP000184191; Unassembled WGS sequence.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:SHL51708.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003693}; Transferase {ECO:0000313|EMBL:SHL51708.1}.
FT   DOMAIN          40..390
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   397 AA;  44226 MW;  DCE7B63236507556 CRC64;
     MEQTIISKSQ LISDRSCNLE MSAIKQMSIL NAKVPDAASL AWGLPSFRTP APIRTATKQA
     LENDPKAGMY ALPGGLPELC VAAAREHEHR TGQCVDPDKQ VMISAGNMEG LQTLFHAIVD
     QGDEVIVTDP GFVSHISQIR FNGGVPVFWP MKEARRWDLD IDALPELISP KTKAIVLVNP
     SNPTGAILSR RTLQGAARIA RAHGILIIID DPYSHFVYDN RDRFFNLASD PSVADCIAYL
     FTFSKAYAMS GWRVGYMVVP EALRNEIVKI HDLTMICTPR ISQIAALAAL ENEPVHLVEF
     ERILDRRRAL ICERLDRLPH VFSYVRPQGA YYVFPRVLVR HDNADRFARD LLDQVHVTVT
     PGSAFGPSGE NHVRMAYCVE DDVINLAFDR LEAHFGA
//