ID A0A1M6IHQ9_9FLAO Unreviewed; 396 AA.
AC A0A1M6IHQ9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=SAMN04487908_11450 {ECO:0000313|EMBL:SHJ33968.1};
OS Aequorivita viscosa.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=797419 {ECO:0000313|EMBL:SHJ33968.1, ECO:0000313|Proteomes:UP000184172};
RN [1] {ECO:0000313|Proteomes:UP000184172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26349 {ECO:0000313|Proteomes:UP000184172};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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 -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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; FQYV01000014; SHJ33968.1; -; Genomic_DNA.
DR RefSeq; WP_073218616.1; NZ_FQYV01000014.1.
DR AlphaFoldDB; A0A1M6IHQ9; -.
DR STRING; 797419.SAMN05216556_10752; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000184172; 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: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; 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; 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.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:SHJ33968.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184172};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:SHJ33968.1}.
FT DOMAIN 33..390
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 396 AA; 43926 MW; 4B4924F29C4DF4C9 CRC64;
MDNRLSKRVN EMETSATLAM AAKTRELKDQ GVDIIGLSLG EPDFTVPEYI KEAAIQAIKD
DFHAYTPVDG YADLKQAIIT KFKRDNNLSY KPSQIVVSTG AKQSLANLTM VLLNEGDEVL
LPAPYWVSYA DQCKVAGGIP KEIPTSIETD FKVTAEALEA AITPKTKLIL YSSPCNPSGS
VYSRKELRKL ADVLVKYPDV IVISDEIYEH INFTGKHASM AEFEDMYDRT VVVNGVSKAF
AMTGWRIGYI GGPEWIARAC NKMQGQVTSG TNCIAQRAAI TALENPPSKI KFMVDAFKER
RRIILDLLSD IKGIKTNEPE GAFYVFPDVS YFFGKTLRGK HINTASDFSL YLLEEARVAT
VTGEAFGDPN CIRLSYAASE KEIREAIKRI KEALEE
//