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Database: UniProt
Entry: A0A0D6MV93_ACEAC
LinkDB: A0A0D6MV93_ACEAC
Original site: A0A0D6MV93_ACEAC 
ID   A0A0D6MV93_ACEAC        Unreviewed;       449 AA.
AC   A0A0D6MV93; A0A7G1M9K1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Aminotransferase, beta alanine--pyruvate transaminase {ECO:0000313|EMBL:GAN57594.1};
GN   ORFNames=Abac_018_007 {ECO:0000313|EMBL:GAN57594.1};
OS   Acetobacter aceti NBRC 14818.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter; Acetobacter subgen. Acetobacter.
OX   NCBI_TaxID=887700 {ECO:0000313|EMBL:GAN57594.1, ECO:0000313|Proteomes:UP000032677};
RN   [1] {ECO:0000313|EMBL:GAN57594.1, ECO:0000313|Proteomes:UP000032677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 14818 {ECO:0000313|EMBL:GAN57594.1,
RC   ECO:0000313|Proteomes:UP000032677};
RA   Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT   "Whole genome sequence of Acetobacter aceti NBRC 14818.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAN57594.1}.
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DR   EMBL; BAMU01000018; GAN57594.1; -; Genomic_DNA.
DR   RefSeq; WP_010665877.1; NZ_SLZP01000005.1.
DR   AlphaFoldDB; A0A0D6MV93; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000032677; Unassembled WGS sequence.
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; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42684:SF1; BETA-ALANINE--PYRUVATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
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:GAN57594.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Pyruvate {ECO:0000313|EMBL:GAN57594.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:GAN57594.1}.
SQ   SEQUENCE   449 AA;  49039 MW;  4ECD05F73CFCB8C6 CRC64;
     MSELKNEFDC ARSLKEGRYW MPFTANRRVK EQGMARVLES ASGPYYTTAD GVKLFDTLSG
     LWCSPLGHAD PRISETLKKQ ADTLDYAPGF QLANPVTVRL AERIANMAPA GLEHVFFANS
     GSEAADTALK AAIGYHRLRG EGGRFRLIGR ERGYHGVGLG GMSVGGIVPN RKMFATIMVP
     GVDHIRHPYD HARVAFSKGQ PEWGAEMAED LERVIALHDA STIAAVMVEP VQGSTGVLVP
     PIGYLERLRE ICTKHGILLI FDEVITGFGR MGENFASQRF GVKPDMITFA KAVTNGIVPM
     GGVIVTDEIY NTFMTGPENA IEFAHGYTYS GHPLAAAVAH TVLDIMEEES LIARARSLEP
     VLEEAIHSLR DLPIVHDIRN IGLTAGVDLK PRKDAPGARC LELFEKGLKN GLLLRCTGET
     ISFGPPFIST PEQLRDMVAT VRKLITELD
//
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