ID A0A2I8DPM8_9BURK Unreviewed; 458 AA.
AC A0A2I8DPM8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:AUT49353.1};
GN ORFNames=C2U31_27225 {ECO:0000313|EMBL:AUT49353.1};
OS Achromobacter sp. AONIH1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=1758194 {ECO:0000313|EMBL:AUT49353.1, ECO:0000313|Proteomes:UP000236176};
RN [1] {ECO:0000313|Proteomes:UP000236176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AONIH1 {ECO:0000313|Proteomes:UP000236176};
RX PubMed=29437920;
RG NISC Comparative Sequencing Program;
RA Weingarten R.A., Johnson R.C., Conlan S., Ramsburg A.M., Dekker J.P.,
RA Lau A.F., Khil P., Odom R.T., Deming C., Park M., Thomas P.J.,
RA Henderson D.K., Palmore T.N., Segre J.A., Frank K.M.;
RT "Genomic Analysis of Hospital Plumbing Reveals Diverse Reservoir of
RT Bacterial Plasmids Conferring Carbapenem Resistance.";
RL MBio 9:e02011-e02017(2018).
RN [2] {ECO:0000313|Proteomes:UP000236176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AONIH1 {ECO:0000313|Proteomes:UP000236176};
RA Segre J.A., Mullikin J.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP026124; AUT49353.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I8DPM8; -.
DR KEGG; achr:C2U31_27225; -.
DR OrthoDB; 3398487at2; -.
DR Proteomes; UP000236176; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00610; OAT_like; 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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:AUT49353.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000236176};
KW Transferase {ECO:0000313|EMBL:AUT49353.1}.
SQ SEQUENCE 458 AA; 51170 MW; 86D51A2C8F3DF287 CRC64;
MSIDTASLLA DEARYCSFGD TVHYVNPPKI FTGCEGSYMY DDAGTAYLDL QMWYSAVNFG
YKNKRLEQKM IEQLQSLPQV ASQYLHPTKI ELAKFIAQDA EKKWGHTGRV HFNVGGAQAI
EDSLKVVRNA SGGKSLMFAF EGGYHGRTLG ASSITSSYRY RRRYGHFGDR AQFIPFPYPF
RRPKGMTAEE YSDSIVKEFA RKFENEYHAI WDPKTNQCEY AAFYVEPIQG TGGYVVPPPN
FFKGLKKVLD DHGVLLVVDE IQMGFWRTGT LWSVENFGVK PDVLVFAKAL TNGLNALSGL
WAREELINPT LFPPGSTHST FASNPLGTAL GLEVMKMTHE MDFGRQVRES GAYFLEGLRD
LQKRHREIGD VDGLGLALRA EICTEDGFTP NKALLDKMVD IGLAGDLDFQ GGKRGLVLDV
GGYYKNVITF APSLMISRSE IDEAMALLDQ LISRAKRA
//
