ID Q2KXX1_BORA1 Unreviewed; 451 AA.
AC Q2KXX1;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Class III aminotransferase {ECO:0000313|EMBL:CAJ48195.1};
GN OrderedLocusNames=BAV0590 {ECO:0000313|EMBL:CAJ48195.1};
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ48195.1, ECO:0000313|Proteomes:UP000001977};
RN [1] {ECO:0000313|EMBL:CAJ48195.1, ECO:0000313|Proteomes:UP000001977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N {ECO:0000313|EMBL:CAJ48195.1,
RC ECO:0000313|Proteomes:UP000001977};
RX PubMed=16885469; DOI=10.1128/JB.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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; AM167904; CAJ48195.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2KXX1; -.
DR STRING; 360910.BAV0590; -.
DR KEGG; bav:BAV0590; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_0_4; -.
DR Proteomes; UP000001977; 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; PTHR43094; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CAJ48195.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000001977};
KW Transferase {ECO:0000313|EMBL:CAJ48195.1}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 48021 MW; C765FE9E81FD4354 CRC64;
MSTGSVMTHI FHRNPRKPPS LAVRGQGSFL IDAQGKRYFD GSGGAAVSCL GHGHAEVIEA
VIEQIRNLEY AHTGFFSSEP AEALAELLAR ESPASLGNVY FLSSGSEAVE TALKMARQYH
VERGQRERRH TIARLQSYHG NTLGALAIGG HRGRRALYQP LLPQSSHVSA CFARHYRMPG
EDDHTYGDRL AAELEQRILE LGPETVSAFI AETVVGATAG AVCAVPGYFA KIRRVCDRYG
VLLILDEVMS GMGRTGTYHA FEAEGVVPDL LCLAKGLGGG YQPIAAVLAQ DRVVETIVAG
SGAFQHGHTY VGHPVACAGA LAVQRIVARD GLVAQSARLG DYLHTRLQAQ FGGHPHVGDI
RGRGLFQAIE LVARRAPDEP FDAALQVHAR IKLAAQALGL LCYPGGGTID GERGDHVLLA
PPYTASTGEL DFAVEGLAQA LDTVIAGLSV K
//
