ID A0A1E7ETD8_9STRA Unreviewed; 448 AA.
AC A0A1E7ETD8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=4-aminobutyrate transaminase {ECO:0000313|EMBL:OEU09290.1};
GN ORFNames=FRACYDRAFT_212372 {ECO:0000313|EMBL:OEU09290.1};
OS Fragilariopsis cylindrus CCMP1102.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Bacillariales; Bacillariaceae;
OC Fragilariopsis.
OX NCBI_TaxID=635003 {ECO:0000313|EMBL:OEU09290.1, ECO:0000313|Proteomes:UP000095751};
RN [1] {ECO:0000313|EMBL:OEU09290.1, ECO:0000313|Proteomes:UP000095751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1102 {ECO:0000313|EMBL:OEU09290.1,
RC ECO:0000313|Proteomes:UP000095751};
RG DOE Joint Genome Institute;
RA Mock T., Otillar R.P., Strauss J., Dupont C., Frickenhaus S., Maumus F.,
RA Mcmullan M., Sanges R., Schmutz J., Toseland A., Valas R., Veluchamy A.,
RA Ward B.J., Allen A., Barry K., Falciatore A., Ferrante M., Fortunato A.E.,
RA Gloeckner G., Gruber A., Hipkin R., Janech M., Kroth P., Leese F.,
RA Lindquist E., Lyon B.R., Martin J., Mayer C., Parker M., Quesneville H.,
RA Raymond J., Uhlig C., Valentin K.U., Worden A.Z., Armbrust E.V., Bowler C.,
RA Green B., Moulton V., Van Oosterhout C., Grigoriev I.;
RT "Extensive genetic diversity and differential bi-allelic expression allows
RT diatom success in the polar Southern Ocean.";
RL Submitted (SEP-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 -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; KV784376; OEU09290.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E7ETD8; -.
DR EnsemblProtists; OEU09290; OEU09290; FRACYDRAFT_212372.
DR KEGG; fcy:FRACYDRAFT_212372; -.
DR InParanoid; A0A1E7ETD8; -.
DR OrthoDB; 345661at2759; -.
DR Proteomes; UP000095751; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000095751}.
SQ SEQUENCE 448 AA; 48849 MW; 83800EFB60B824C8 CRC64;
MIRRCWNSTT TTKTSTKGTG QHLSSVWSHL TTIQPVRGKG IYLYDADGTK YSDFTSGIGV
TNLGHCHPKV VSAIQEQVTK LHFGQMNVVM TPQFIELSEK LYDITPDGID SFFFANSGAE
ATEAAVKLAR HASGKTNIVV FNGSFHGRTT QCMAMTTSKY IYRENYAPLP GNIHVTPFPH
SYYYGWDEKT TIDFCMKELH RLVVSQTSVD ETAAIFVEPV LGEGGYVPVP NEFMKLLREF
CDQHEILLVM DEIQSGFGRT GKMFAVNHSG VKPDIMVMAK GLGNGMPISA VGASTELMSK
WKAGTHGGTY GGGNALVAKA ALATIDAMLE ENIPARAADR GEYLMTKLRG VQDRNPILGD
VRGLGLMVGT EFTDPITGEP AGDIAKAVRT GCIENNLLIL TCGTNDHVIR WIPPLIVTEA
QIDEAVDVFE RVINDVTDCF SSDEEGMG
//