ID A0A2N7DAG7_9VIBR Unreviewed; 396 AA.
AC A0A2N7DAG7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=BCU70_11115 {ECO:0000313|EMBL:PMH40702.1};
OS Vibrio sp. 10N.286.49.C2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1880856 {ECO:0000313|EMBL:PMH40702.1, ECO:0000313|Proteomes:UP000235640};
RN [1] {ECO:0000313|Proteomes:UP000235640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10N.286.49.C2 {ECO:0000313|Proteomes:UP000235640};
RA Kauffman K., Hussain F., Yang J., Arevalo P., Brown J., Cutler M.,
RA Kelly L., Polz M.F.;
RT "Nontailed viruses are major unrecognized killers of bacteria in the
RT ocean.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000481};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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:PMH40702.1}.
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DR EMBL; MCUT01000025; PMH40702.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N7DAG7; -.
DR OrthoDB; 9766445at2; -.
DR Proteomes; UP000235640; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; 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; IPR000796; Asp_trans.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR11879:SF22; ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:PMH40702.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:PMH40702.1}.
FT DOMAIN 27..392
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 396 AA; 42963 MW; DA2C54806B603654 CRC64;
MFEKVVAAPA DPILGLTEEF KKDTRAEKIN LGVGIYKNEQ GQTPVLATVK KAEAALLENE
KTKSYLTIEG TAEYGLAVQK LLFGEESQIV TQKLAKTAQA PGGTGALRVA GEFIKRQLTG
AKIWISNPTW ANHNGVFAAA GIETAQYSYY NSESKDKDFA GMVADLEQAS AGDIVLLHGC
CHNPTGIDPT LPEWEQLAKL VADKGLIPLF DFAYQGFAKG VEEDAQGLRI FAKHNKEILV
ASSFSKNFGL YNERVGAFTL VAASNDIAET AFSQVKGIIR SIYSNPPAHG AAVVTYILND
AALRAEWENE VAEMRDRIQE MRGLFVETLK AEGVNADFSF IERQNGMFSF SGLSKEQVNQ
LKDEFAIYIV GSGRISVAGM TKSNMTPLCK GIAAVL
//
