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Database: UniProt
Entry: F9YQ33_CAPCC
LinkDB: F9YQ33_CAPCC
Original site: F9YQ33_CAPCC 
ID   F9YQ33_CAPCC            Unreviewed;       417 AA.
AC   F9YQ33;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Transaminase A {ECO:0000313|EMBL:AEK23452.1};
DE            EC=2.6.1.1 {ECO:0000313|EMBL:AEK23452.1};
GN   OrderedLocusNames=Ccan_13360 {ECO:0000313|EMBL:AEK23452.1};
OS   Capnocytophaga canimorsus (strain 5).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=860228 {ECO:0000313|EMBL:AEK23452.1, ECO:0000313|Proteomes:UP000008895};
RN   [1] {ECO:0000313|EMBL:AEK23452.1, ECO:0000313|Proteomes:UP000008895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5 {ECO:0000313|Proteomes:UP000008895};
RX   PubMed=21914877; DOI=10.1128/JB.05853-11;
RA   Manfredi P., Pagni M., Cornelis G.R.;
RT   "Complete genome sequence of the dog commensal and human pathogen
RT   Capnocytophaga canimorsus strain 5.";
RL   J. Bacteriol. 193:5558-5559(2011).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR   EMBL; CP002113; AEK23452.1; -; Genomic_DNA.
DR   RefSeq; WP_013997441.1; NC_015846.1.
DR   AlphaFoldDB; F9YQ33; -.
DR   STRING; 860228.Ccan_13360; -.
DR   KEGG; ccm:Ccan_13360; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_3_10; -.
DR   OrthoDB; 9813612at2; -.
DR   Proteomes; UP000008895; Chromosome.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:AEK23452.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008895};
KW   Transferase {ECO:0000313|EMBL:AEK23452.1}.
FT   DOMAIN          31..408
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   417 AA;  46322 MW;  6AAEDC9520024A10 CRC64;
     MKVSKLAQNL IGSEIVKIGN EVNDLKAKGE KITNLTIGDL DSNIYPIPNE LKKGIQQAYA
     DNLTNYPPAS GILSLRENVS KDLKQRYALE YSAKDILIAG GSRPLIYATF KTIVDEGDKV
     IYPVPSWNNN HYSYLNSAQK IELEVKPENN FLPTAEELRP HLKDAVLLAL CSPLNPTGTM
     FSEHQLREIC ELIVEENRKR GADEKPLYLM YDQIYAMLTF GEKHFNPVSL VPEMKPYTIF
     IDGSSKCFAA TGVRVGWAFG PSEIIGKMAA LLTHVGAWAP KPEQQAMAQF LTNTKAVDAF
     VNDFKGKIKH SLETLHEGIQ ALKQKGYAVE SIRPMGALYL TIQLDYVGKT TPKGDKLNDT
     TDLVFYLIKE AGMALVPFSA FGNSRTMPWF RASAGGCSLQ DIKDVLPRLE KALSELK
//
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