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Database: UniProt
Entry: A0A2E7P1I0_9BURK
LinkDB: A0A2E7P1I0_9BURK
Original site: A0A2E7P1I0_9BURK 
ID   A0A2E7P1I0_9BURK        Unreviewed;       402 AA.
AC   A0A2E7P1I0;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=CME87_08010 {ECO:0000313|EMBL:MBO15413.1};
OS   Herbaspirillum sp.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=1890675 {ECO:0000313|EMBL:MBO15413.1, ECO:0000313|Proteomes:UP000226028};
RN   [1] {ECO:0000313|Proteomes:UP000226028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Graham E.D., Heidelberg J.F.;
RT   "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT   Global Oceans.";
RL   Submitted (SEP-2017) 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:MBO15413.1}.
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DR   EMBL; PBPP01000052; MBO15413.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2E7P1I0; -.
DR   Proteomes; UP000226028; 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:MBO15413.1};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:MBO15413.1}.
FT   DOMAIN          33..393
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   402 AA;  43402 MW;  E071A37A64FC6667 CRC64;
     MTSPRIADRV RRIKQSPSSA AAERAAELRR QGKDIVNLVV GEPDFDTPAH IRRAAAEAIE
     SGQTRYTPTA GTPALRQAIS EKLARENQLA YAPREIIATC GAKHAIFNAL AITVQTGDEV
     LVPAPYWVSY PDMVLACDGT PVVVPCVEED GFKLTPAVLD AAITARTKWL IINSPSNPTG
     AAYTLEELQA LAEVLRRHPQ VLVMTDDIYE HIRFDGQPTP HLLNAAPDLR ERTLLINGVS
     KTYAMTGWRI GYAAGPSDLI GALDILQSQS TSNPSSVSQA AALAALTGDQ GFVAEFADTY
     RRRRDRGLEL INAIDGLSCR KPEGAFYLFI NCSGLLGRRT PEGKVIESDT DVVMYFLEST
     GVALVAGTAY GLSPYMRMSI ATAVETIEEG CRRMAGAVAA LR
//
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