ID A0A1G6MRB2_9BURK Unreviewed; 402 AA.
AC A0A1G6MRB2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=SAMN05444679_10416 {ECO:0000313|EMBL:SDC58128.1};
OS Variovorax sp. CF079.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1882774 {ECO:0000313|EMBL:SDC58128.1, ECO:0000313|Proteomes:UP000198763};
RN [1] {ECO:0000313|EMBL:SDC58128.1, ECO:0000313|Proteomes:UP000198763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF079 {ECO:0000313|EMBL:SDC58128.1,
RC ECO:0000313|Proteomes:UP000198763};
RA de Groot N.N.;
RL Submitted (OCT-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; FMZU01000004; SDC58128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6MRB2; -.
DR STRING; 1882774.SAMN05444679_10416; -.
DR OrthoDB; 9803354at2; -.
DR Proteomes; UP000198763; 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:SDC58128.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198763};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:SDC58128.1}.
FT DOMAIN 34..394
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 43215 MW; F6C678D9E016567A CRC64;
MTTSRIAARV RRIKPSPSTS AADRANELRR QGKSIVNLVV GEPDFDTPLH IRRAAAEAMD
KGATRYTLMA GTVELRQAIV AKLERENGLS YALNEIIVTS GAKSAIYNAF AITLEPGDEV
IIPAPYWVSY PDMVLACEGK PVIVACPEAH GFKLTPAQLE AAITPRTRWL LINSPSNPTG
ASYTADEYRA LADVLMRHPH VMVMTDDIYE HIRFDGRSTP HILATEPSLR ERTLAVNGVS
KTYAMTGWRI GWAAGPADLI TAMDTLLSQS AGNCCSISQA AAAAALNSDQ SFVAESVAVY
KERRDRTLAL VNAIPGLSCA TPPGAFYLYI HCAGLIGKTT PAGKQLNEDG DVVMYLLESA
GVATVAGTAY GLSPYFRLSI ATSIETLEEG CTRIARAVAE LR
//