ID   A0A0P1IFC9_9RHOB        Unreviewed;      1021 AA.
AC   A0A0P1IFC9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Acetylornithine/acetyl-lysine aminotransferase {ECO:0000313|EMBL:CUK09884.1};
DE            EC=2.6.1.- {ECO:0000313|EMBL:CUK09884.1};
GN   Name=argD {ECO:0000313|EMBL:CUK09884.1};
GN   ORFNames=RUE5091_03241 {ECO:0000313|EMBL:CUK09884.1};
OS   Ruegeria denitrificans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=1715692 {ECO:0000313|EMBL:CUK09884.1, ECO:0000313|Proteomes:UP000051260};
RN   [1] {ECO:0000313|EMBL:CUK09884.1, ECO:0000313|Proteomes:UP000051260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5091 {ECO:0000313|EMBL:CUK09884.1,
RC   ECO:0000313|Proteomes:UP000051260};
RG   Swine Surveillance;
RL   Submitted (SEP-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   ---------------------------------------------------------------------------
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; CYUD01000010; CUK09884.1; -; Genomic_DNA.
DR   RefSeq; WP_058282915.1; NZ_CYUD01000010.1.
DR   AlphaFoldDB; A0A0P1IFC9; -.
DR   STRING; 1715692.RUE5091_03241; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000051260; 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; cd12797; M23_peptidase; 1.
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; IPR016047; Peptidase_M23.
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   Pfam; PF01551; Peptidase_M23; 1.
DR   SUPFAM; SSF51261; Duplicated hybrid motif; 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:CUK09884.1};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Transferase {ECO:0000313|EMBL:CUK09884.1}.
FT   DOMAIN          25..269
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
FT   DOMAIN          431..529
FT                   /note="Peptidase M23"
FT                   /evidence="ECO:0000259|Pfam:PF01551"
SQ   SEQUENCE   1021 AA;  111852 MW;  7DA5CC5982A3F054 CRC64;
     MSDLTEFWAD ALRAHWGLDA KLERLDGEYD LNFMVRATNG QDYVLKVMRP GCEAEFVDLQ
     VKALGHIAAE APGLPFPQVY PDLNGAQLPE IADQQGQLRL VWLLECLPGQ CYAKAARKSE
     ALILKLGRVL GATDKALERF AHDGLHRADF KWDLTQAGWI ADRLDAIADP TRRAVLSVIC
     DKFAAISGPL AGLPKQAIHN DANDYNILVE GELGQRQSIS GLIDLGDMCA APRVCDLAIA
     GAYIVLDHPT SERALTALVQ GYHAANRLRP DEIDLIWPLL QMRLAVSVVN STLMAAENPD
     DPYVTISQAP AWRFLENAGV NGDLMSARLR TACGLPVTDG AERIHAYLSE HRGQFAQMFE
     EDLSDVPMGS LSVENSTWPQ NPFHMPLEEA ARVGEEFGEG LWLGYYNEPR LIYAEPGFRK
     GPWKASDRRT VHLAVDVFAP AGTVLHAPMS GRVEAVENRD AHLDYGGVVI LHHETPEGDP
     FYTLYGHLDP EVSARLKPGD PVAQGAAFAR LGDASQNGGW APHVHFQLAL TTDGMQTDWP
     GVGDPDEMEL WHAVCPNPAA LLNLADEKVF YRPTDKQVIL QGRHDHFGGN LSLTYDDPVM
     LVRGWRHHLF DEWGRPYLDA YNNVPHVGHA HPRIQVVASD QLKRMNSNTR YLHPAQTAFA
     DKILSKLPDQ FEVCFFVNSG TEANELALRL ARAHTGAKGI VTPDHGYHGN TNAAVAISAY
     KFNKPGGVGQ AEWVELVEVA DDYRGSFKRN DPDRAQKYAD LVDPAIAALQ DKGQGVAGFI
     AETFPSVGGQ IIPPKGYLPA VYEKIRAAGG VCIADEVQTG LGRLGDFYFG FEHQGALPDI
     VVMGKPIGNG HPLGVLVTTK EIAQSFDNGI EFFSTFGGST LSCRIGKEVL DIVDDEGLQD
     NAREMGARLM DGLRQIEAEF GSVGDVRGMG LFLGVELVNP DGSEGTDICK YVKNRMRDHR
     ILIGSEGPKD NILKIRPPLT IEAEDVDMIL WALRDVLTEV GEFNPAPACD HEHHHVGCGC
     C
//