ID   A0A0F2RWT7_9PROT        Unreviewed;       464 AA.
AC   A0A0F2RWT7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Aminotransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=VR70_03125 {ECO:0000313|EMBL:KJS43053.1};
OS   Rhodospirillaceae bacterium BRH_c57.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae.
OX   NCBI_TaxID=1629718 {ECO:0000313|EMBL:KJS43053.1, ECO:0000313|Proteomes:UP000033468};
RN   [1] {ECO:0000313|EMBL:KJS43053.1, ECO:0000313|Proteomes:UP000033468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c57 {ECO:0000313|EMBL:KJS43053.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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:KJS43053.1}.
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DR   EMBL; LAEA01000053; KJS43053.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2RWT7; -.
DR   STRING; 1629718.VR70_03125; -.
DR   PATRIC; fig|1629718.3.peg.496; -.
DR   Proteomes; UP000033468; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}.
SQ   SEQUENCE   464 AA;  49937 MW;  C87C5635C8C3BEE4 CRC64;
     MDPKTLADLR AADRAHLFHP STHMRTHAAG ESPNRIVVGG EGATIIDAEG NRLLDGFAGL
     YCVNIGYGRP EMAQAVARQM TELAYYHAYV GHGSAPAAEL SARVMEWMPA NMRRIYYGLS
     GSDANETQLK LIRYFWNIEG RPEKKKIIAR HRAYHGSGIM TGSLTGLEVF HKPFDLPEAP
     ILHVATPHFA RHGLPGETER DYSKRLAAEL DAFIKAEGPD TVAAFFAEPV MGTGGILPPP
     KGYFDEIVPV LRRHDVLFVA DEVVTAFGRL GAPCGALYYG FEPDLITVAK GMTSAYLPLS
     GAVVSERVWA TLERGSDALG PIGHGWTYSA HPTCAAAGLA NLAILRDENL MERAAEAGRL
     LLSGLREAFD GLPGVFEVRG EGLLAAVEFG LDAKGTPFDP SRKVGPRIAA AMAEDGVIAR
     ALPHGDILAF APPFVIAPEE IERLVSTARR AAERVLKEEG ALAA
//