ID A0A0Q1BYE3_9FLAO Unreviewed; 397 AA.
AC A0A0Q1BYE3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=AAY42_07535 {ECO:0000313|EMBL:KQC29756.1};
OS Allomuricauda eckloniae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=346185 {ECO:0000313|EMBL:KQC29756.1, ECO:0000313|Proteomes:UP000050827};
RN [1] {ECO:0000313|EMBL:KQC29756.1, ECO:0000313|Proteomes:UP000050827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK169 {ECO:0000313|EMBL:KQC29756.1,
RC ECO:0000313|Proteomes:UP000050827};
RA Kwon Y.M., Kim S.-J.;
RT "Complete genome of flavobacterium.";
RL Submitted (APR-2015) 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 -!- 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:KQC29756.1}.
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DR EMBL; LCTZ01000002; KQC29756.1; -; Genomic_DNA.
DR RefSeq; WP_055393846.1; NZ_LCTZ01000002.1.
DR AlphaFoldDB; A0A0Q1BYE3; -.
DR STRING; 346185.AAY42_07535; -.
DR PATRIC; fig|1547436.3.peg.1551; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000050827; 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:KQC29756.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050827};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KQC29756.1}.
FT DOMAIN 32..391
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 397 AA; 43500 MW; 7E77EB140F8637AF CRC64;
MSNQLSERIN NLVPSATLAM AAKARELRAS GKDIIGLSLG EPDFNTPDYI KEAAIQAVND
GYNSYTPVDG YVELKDAIIT KFKRDNDISY DHSQIVVSTG AKQALYNLAQ ACLNKGDEVI
LPCPYWVSYS DIVKLADGVP VEVATSIDTD FKMTPEQLEA AITPKTKMLW YSSPCNPSGS
IYSKEELRRL ADVLQKYPQI VVVSDEIYEH INYGVTAHAS MGAFEDMYER TVTVNGVAKA
FAMTGWRIGY IGAPAYIARA CNKLQGQVTS GANCIAQRAV ITALLESPSR IQYMVDEFKN
RRKLILGLLN DIDGFKCNEP EGAFYVYPDV TAFFGKTLNG KTINNASDFA MYLLEEANVA
TVTGDAFGNG NSIRISYAAS EEDIREAISR IAEAVGQ
//