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
//