ID G2FSK9_9FIRM Unreviewed; 388 AA.
AC G2FSK9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=DOT_2685 {ECO:0000313|EMBL:EGW39400.1};
OS Desulfosporosinus sp. OT.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW39400.1, ECO:0000313|Proteomes:UP000004928};
RN [1] {ECO:0000313|EMBL:EGW39400.1, ECO:0000313|Proteomes:UP000004928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT {ECO:0000313|EMBL:EGW39400.1,
RC ECO:0000313|Proteomes:UP000004928};
RX PubMed=21994931; DOI=10.1128/JB.06018-11;
RA Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.;
RT "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate-
RT Reducing Bacterium from Copper Mining Waste in Norilsk, Northern Siberia.";
RL J. Bacteriol. 193:6104-6105(2011).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {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:EGW39400.1}.
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DR EMBL; AGAF01000124; EGW39400.1; -; Genomic_DNA.
DR AlphaFoldDB; G2FSK9; -.
DR PATRIC; fig|913865.3.peg.2475; -.
DR eggNOG; COG0436; Bacteria.
DR Proteomes; UP000004928; 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; 2.
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; PTHR42691; ASPARTATE AMINOTRANSFERASE YHDR-RELATED; 1.
DR PANTHER; PTHR42691:SF1; ASPARTATE AMINOTRANSFERASE YHDR-RELATED; 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:EGW39400.1};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:EGW39400.1}.
FT DOMAIN 29..378
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 388 AA; 43385 MW; 6483E555F35B186A CRC64;
MQEQVKSSSV IRAMFEEGKR LAEIHGAENV FDFSIGNPNV EPPEEINKAI LEILNTEHPM
SIHGYMNNSG YEEVRATIAK SINDKFGTAF TQKNILMTVG AAGGLNVIFK TLLNPQDEVI
TFAPFFGEYR NYVKNYEGEL VIVSPNTVDF QPNLEEFKAK ITPKTKAVII NSPNNPTGVV
YSEETIIKLS EILSEKQKEF GTDIYLVSDE PYRELAYDNV EVPYLTKYYA NTIIGYSFSK
SLSLPGERIG YLVISDQAAD YENIISAANI ANRILGYVNA PSLFQRVVAK CLNAKVDIDT
YNKNRELLFN GLSSYGYECI KPEGAFYLFV KTPIENDVEF CNLAKKKNIL IVTGTAFGCP
GYVRIAYCVA YKTIEKALPA FKALIEEV
//
