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Database: UniProt
Entry: K5YVD8_9PROT
LinkDB: K5YVD8_9PROT
Original site: K5YVD8_9PROT 
ID   K5YVD8_9PROT            Unreviewed;       782 AA.
AC   K5YVD8;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:EKM98792.1};
GN   ORFNames=MXAZACID_13958 {ECO:0000313|EMBL:EKM98792.1};
OS   Acidocella sp. MX-AZ02.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidocella.
OX   NCBI_TaxID=1214225 {ECO:0000313|EMBL:EKM98792.1, ECO:0000313|Proteomes:UP000006217};
RN   [1] {ECO:0000313|EMBL:EKM98792.1, ECO:0000313|Proteomes:UP000006217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MX-AZ02 {ECO:0000313|EMBL:EKM98792.1,
RC   ECO:0000313|Proteomes:UP000006217};
RX   PubMed=23405365;
RA   Servin-Garciduenas L.E., Garrett R.A., Amils R., Martinez-Romero E.;
RT   "Genome Sequence of the Acidophilic Bacterium Acidocella sp. Strain MX-
RT   AZ02.";
RL   Genome Announc. 1:E00041-12(2013).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954}.
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:EKM98792.1}.
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DR   EMBL; AMPS01000193; EKM98792.1; -; Genomic_DNA.
DR   AlphaFoldDB; K5YVD8; -.
DR   STRING; 1214225.MXAZACID_13958; -.
DR   HOGENOM; CLU_010757_1_1_5; -.
DR   Proteomes; UP000006217; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1200.10; -; 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; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:EKM98792.1};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006217};
KW   Transferase {ECO:0000313|EMBL:EKM98792.1}.
FT   DOMAIN          60..288
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
SQ   SEQUENCE   782 AA;  83584 MW;  B6D9D434908E45AC CRC64;
     MCFKVWRAAI GFAYLRAMTD PKSLLALETS PPCFSAEAAA AFARDIFGID GPAKPLYGER
     DQNFRITPAQ GPGIILKILS PTELESAVDF QTIVLDHIQA MDPSLPVPRV RRTLAGDAYA
     FVKDAADTPH MVRALDFQPG RVMDDVEPPP ALLRDVGAQL ARLDRALANV FHPGMGQKIV
     WDLRAIEILR PSAALIEPAQ DRALVEAVLE RFLAFRPHLD RLRHQPVHND LHPGNMLVDA
     DATRLTGMLD FGDMIHAPLI FDIAVTAAET VGTSLDPIAY ATEIVAGYDA VNPLQPEEFG
     ALFEAIIARH ALAATIMAWR KQNDPEGAEK LAALAGIGIA AIQAFLAAGK ERVVARFRAA
     CASRPSAGLT ARRFAVLGKG LELSYEEPVH LVYGQGAHLF APDGTDYLDA YNNVPSVGHG
     NVRVADAISR QMHWMCTNTR YLHETVVAYA ERLTATLPDG LSQVLFVNSG SEANDTAYRI
     AKAVTGKSGA IVISGAYHGI TEISAALSPY HGPQAQPLEP YIEVLEVPDP FRGRFTEAAP
     YAADADRAIA ALQAKGLGVA MLLVDSAFTA HGITAAPAGY FAAIAAKVRE AGGLVVGDEV
     QSGFGRMGEA FWGFARHGVV PDMVTLGKPM ANGHPTGAVV TRPEILEIFQ RKIEFFSTFG
     GNPVSAAAAL ATLNVLQEED LQGNAQRTGT ALRAGIASLQ GRFPLLADVR GAGLMTGVEI
     FEAGQPSRAL AKRIANAMRR AQVLIGTEGP QGNVLKIRPP LPFNGADATR FLETLERVLA
     GL
//
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