ID A0A0D6PE29_9PROT Unreviewed; 771 AA.
AC A0A0D6PE29;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:GAN79927.1};
GN ORFNames=Aam_034_071 {ECO:0000313|EMBL:GAN79927.1};
OS Acidocella aminolytica 101 = DSM 11237.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidocella.
OX NCBI_TaxID=1120923 {ECO:0000313|EMBL:GAN79927.1, ECO:0000313|Proteomes:UP000032668};
RN [1] {ECO:0000313|EMBL:GAN79927.1, ECO:0000313|Proteomes:UP000032668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=101 / DSM 11237 {ECO:0000313|Proteomes:UP000032668};
RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT "Whole genome sequence of Acidocella aminolytica 101 = DSM 11237.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:GAN79927.1}.
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DR EMBL; BANC01000034; GAN79927.1; -; Genomic_DNA.
DR RefSeq; WP_052948337.1; NZ_FQVJ01000005.1.
DR AlphaFoldDB; A0A0D6PE29; -.
DR STRING; 1120923.SAMN02746095_00856; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000032668; 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:GAN79927.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000032668};
KW Transferase {ECO:0000313|EMBL:GAN79927.1}.
FT DOMAIN 42..266
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
SQ SEQUENCE 771 AA; 82759 MW; AABAAB441132C779 CRC64;
MTDPTNLVAL QTSPPAFTKE AAEQMAGEIF GVPGEARQLY GERDQNFRIK TADGPGIIFK
ILGPSELPEA VEFQIAALDH IKMMDASLPV PRVYRTADGA AYVYVKDAAG TPHMVRALGF
QPGQVMDAIT PTPGLLRDVG ATLARLNQAM ANFFHPGAGQ KIVWDLRAIE TMRPFASLIE
PVEDRALVEA VLDRFLAFRP ALAKLRHQPV HNDLHPGNML VNEDASRVTG LLDFGDMIHG
PLIFDLAVTA AETVGENLDP ITYATHVIAG YDAVNTLEPA EFEALYEAII ARHALAATIM
AWRKQNDPSG AEKLAALASI GIAAIQAYQA EGKEKVVARF RAASAAPLEV DSAALAARRF
NVLGKGLELS YEQPVHLVYG QGVHLYAPDG TDYLDAYNNV PSVGHGNARV AEAISRQMRR
LCANTRYLHE NVVEYAERLT ATLPDGLAHV LFVNSGSEAN DAAYRIAKAL TGKTGAIVMA
NAYHGITDVV AALSPYYGPF AQKQEDFIEV LESPDPFRGR FSGPEAGAAY ARDVDRAIAA
LEARGHGVAM LLIDSAFVSN GIVDTPPGYF TAVAEKVRAA GGLVVGDEVQ SGFGRMGETF
WGFARHGVVP DMVTLGKPMA NGHPTGALVT RPEILADFTR KIDFFSTFGG NPVSAAAALA
TLEVLQQEKL QQNARKTGEF LRNELAGLQV EFPLLADVRG AGLMVGVEIY EEGQPSQKLA
KRIANGLRQA RVLIGTEGPD GNVLKIRPPL PFATQDAARL VEALRGVLRG L
//