ID   A3X4F1_9RHOB            Unreviewed;       367 AA.
AC   A3X4F1;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=MED193_21099 {ECO:0000313|EMBL:EAQ47731.1};
OS   Roseobacter sp. MED193.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=314262 {ECO:0000313|EMBL:EAQ47731.1, ECO:0000313|Proteomes:UP000005943};
RN   [1] {ECO:0000313|EMBL:EAQ47731.1, ECO:0000313|Proteomes:UP000005943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED193 {ECO:0000313|EMBL:EAQ47731.1,
RC   ECO:0000313|Proteomes:UP000005943};
RA   Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA   Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.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|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAQ47731.1}.
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; AANB01000001; EAQ47731.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3X4F1; -.
DR   STRING; 314262.MED193_21099; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_3_5; -.
DR   Proteomes; UP000005943; 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; 3.40.640.10; 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:EAQ47731.1};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:EAQ47731.1}.
FT   DOMAIN          16..358
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   367 AA;  39562 MW;  B16EFE09C774966C CRC64;
     MDVMEAARQA EEQGRHIIHM EVGQPSTGAP MAARRALSDA LEDNSLGYTV ALGLPALRQG
     IARLYGEWYN VDLNPDRVVV TPGSSGAFLL GFTALFDSGD RVGIGAPGYP SYRQILSALG
     LTPVDIETAP ENRLQPVASD LEGLDLAGLM VASPGNPTGT MLDRAAMGQL IDAAKAQNAS
     FISDEIYHGL EYEAKAVTAL ELTDECYVIN SFSKFFSMTG WRVGWMVVPE DHVRVIERLA
     QNMFICAPHA SQIAALAALD CQDEMRENLA VYARNRQLML EGLVAAGFDK IAPPDGAFYV
     YADVSDLTTD SRSFAAEILE KAGVAVTPGL DFDPKRGATT LRFSYARGTA DIEEGLSRLK
     QFMAARG
//