ID   A0A2G4YWC3_9PROT        Unreviewed;       978 AA.
AC   A0A2G4YWC3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Aminoglycoside phosphotransferase domain-containing protein {ECO:0000259|Pfam:PF01636};
GN   ORFNames=CRD36_01710 {ECO:0000313|EMBL:PHZ86619.1};
OS   Paremcibacter congregatus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Emcibacterales;
OC   Emcibacteraceae; Paremcibacter.
OX   NCBI_TaxID=2043170 {ECO:0000313|EMBL:PHZ86619.1, ECO:0000313|Proteomes:UP000229730};
RN   [1] {ECO:0000313|EMBL:PHZ86619.1, ECO:0000313|Proteomes:UP000229730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZYL {ECO:0000313|EMBL:PHZ86619.1,
RC   ECO:0000313|Proteomes:UP000229730};
RA   Zhao Z.;
RT   "Frigbacter circumglobatus gen. nov. sp. nov., isolated from sediment
RT   cultured in situ.";
RL   Submitted (OCT-2017) 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:PHZ86619.1}.
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; PDEM01000007; PHZ86619.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G4YWC3; -.
DR   InParanoid; A0A2G4YWC3; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000229730; 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:InterPro.
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; 2.70.70.10; Glucose Permease (Domain IIA); 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; IPR011055; Dup_hybrid_motif.
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   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000229730};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          34..260
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
SQ   SEQUENCE   978 AA;  104783 MW;  114499684C63876B CRC64;
     MGSFDTPSPA YGPAELQDMA ARLFDISGKM KALVGDRDQN VRLTAANGSY VLKIAHPGEG
     RAFLAFQNAA MDHLANVVPQ LPLPRVVQSV RGEAIARWPQ GAGEGHDVRL LTYLPGNLFS
     DVAKTPALLR DLGHFMGQVS RGLQSFGHPG AHRPDFLWSL DNVLLSEPYV SDIAQEGHRD
     LVAGCFAHYR DQVAPRLTDL RMAVIHNDAN DNNLLVAADQ PDQIAGLIDF GDMVFARQVN
     ELAVMLAYAM MDQADPIAAA TQVISGYTAE FPLTETEAEV LFDLAIMRLV MSVCISSHRA
     KDFPDNDYLV ISQAPAFALL DKLHGYDRNW LIALARQAAG FDAVATASAV SALFPPLTPL
     KVTSVDLMSE PRRLVEAGPL SPASLEEIFA LQADGDQATY AISAYGASDT LGTALYLAPG
     SALMSPLAGR VVEVTAQGGE SRVVIAHQAA AEPLFYSSYR WNGNTQVSRN QILSAGEVIG
     EMGGDAPAGR LFLQLMTVLP SLGHAVPESC TAALWPVLKD IYLDPNLTLG LPPETFTSDE
     QGPAEMMAAR RQMLAPSLSV AYARKLKMVR GKGAYLYDHT GRAFLDCVNN ITHVGHCHPH
     VVGALSRQAA LLNTNSRYLS ENIQTLAARI LATLPDPLEV MFFVNSGSEA NELALRLTRA
     MTGRKTMVVL DHAYHGNTSS LVDISPYKFN GKGGAGCPDH VRIADFPDPY QGLYKGDGPD
     AAKAYARETP RSVAQCVADL EATTGAGPGG FIAESIAGVG GQVIYPDGYL AETYKVIRAA
     GGLCIADEVQ VGFGRVGSHM WAFETQGVVP DIVSLGKPIG NGHPLAAVAT TREIAEKFAN
     GMEYFNSFGG NPVSCAVGLA VLDVIENEKL QQKAQDTGDY ILAGLRELAT RWPLIGDVRG
     RGMFIGVELV KDRDSRAPAA EEAGLIVQHL RDHGVLLSTD GPHENVLKLK PPMVFGRAEA
     DIFLTKLDQA FACLAAKK
//