(data stored in SCRATCH zone)

SWISSPROT: A0KEV7_AERHH

ID   A0KEV7_AERHH            Unreviewed;       443 AA.
AC   A0KEV7;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   SubName: Full=Omega-amino acid--pyruvate aminotransferase {ECO:0000313|EMBL:ABK36563.1};
DE            EC=2.6.1.18 {ECO:0000313|EMBL:ABK36563.1};
GN   OrderedLocusNames=AHA_0245 {ECO:0000313|EMBL:ABK36563.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK36563.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK36563.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP000462; ABK36563.1; -; Genomic_DNA.
DR   RefSeq; WP_011704253.1; NC_008570.1.
DR   RefSeq; YP_854773.1; NC_008570.1.
DR   STRING; 380703.AHA_0245; -.
DR   EnsemblBacteria; ABK36563; ABK36563; AHA_0245.
DR   GeneID; 4486946; -.
DR   KEGG; aha:AHA_0245; -.
DR   PATRIC; fig|380703.7.peg.232; -.
DR   eggNOG; ENOG4108JPX; Bacteria.
DR   eggNOG; COG0161; LUCA.
DR   HOGENOM; HOG000020207; -.
DR   KO; K00822; -.
DR   OMA; YTTHVND; -.
DR   BioCyc; AHYD380703:G1G7B-246-MONOMER; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0016223; F:beta-alanine-pyruvate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KEV7.
DR   SWISS-2DPAGE; A0KEV7.
KW   Aminotransferase {ECO:0000313|EMBL:ABK36563.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Pyruvate {ECO:0000313|EMBL:ABK36563.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   Transferase {ECO:0000313|EMBL:ABK36563.1}.
SQ   SEQUENCE   443 AA;  47897 MW;  77D19E59AED36AF6 CRC64;
     MKPISDINTP SDMSAFWMPF TANQQFKAAP RILKSAEGMY YHSEDGRKIL DGTAGLWCCN
     AGHGRREIAE AVSQQISHLD FAPTFQMGHP LPFELANRLV EIAPKGLGHV FYTNSGSESV
     DTALKIALAW QRARGQGTRT RLIGRERGYH GVGFGGISVG GIPGNRKWFG SLLGGVDHLP
     HTLNIAKNAF TKGLPEEDVA LADELEKIVF LHDASNIAAV IVEPIAGSTG VLMPPKGYLK
     RLREICTKHG ILLIFDEVIT GFGRLGAPFA AQEFDVIPDM ITCAKGLTNG AIPMGAVLVS
     NAIYDDMMAA GKGAIELFHG YTYSGHPVAA AAGLATLEIY RNENLLSRAA DLAGYWEEAA
     HSLKGCKHVK DVRNYGLVAG IELESMPDAP GKRAYEVFVR CFEKGALIRV TGDIIALSPP
     LIIERSQIDD LFTLLQDALQ AQD
//

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