ID R7RP90_9CLOT Unreviewed; 386 AA.
AC R7RP90;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=TCEL_01793 {ECO:0000313|EMBL:CDF57879.1};
OS Thermobrachium celere DSM 8682.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Thermobrachium.
OX NCBI_TaxID=941824 {ECO:0000313|EMBL:CDF57879.1, ECO:0000313|Proteomes:UP000014923};
RN [1] {ECO:0000313|EMBL:CDF57879.1, ECO:0000313|Proteomes:UP000014923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8682 {ECO:0000313|EMBL:CDF57879.1,
RC ECO:0000313|Proteomes:UP000014923};
RA Ciranna A., Larjo A., Kivisto A., Santala V., Roos C., Karp M.;
RT "Draft genome sequence of the hydrogen-ethanol-producing anaerobic
RT alkalithermophilic Caloramator celere.";
RL Submitted (MAR-2013) 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|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:CDF57879.1}.
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DR EMBL; CAVN010000092; CDF57879.1; -; Genomic_DNA.
DR RefSeq; WP_018661443.1; NZ_HF952018.1.
DR AlphaFoldDB; R7RP90; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_5_9; -.
DR Proteomes; UP000014923; 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; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42832:SF3; LL-DIAMINOPIMELATE 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:CDF57879.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014923};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000481}.
FT DOMAIN 31..381
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 386 AA; 43896 MW; 4E35FB38FFAC89D6 CRC64;
MKLSNRLNKV PKYIFSRLDE LKAKYKEKGI KVIDLSIGDP DIETPEFVVD FLIESLKNQN
YHKYPPYDGI EELKISIANY YKRRFNVDLN YKDEIAVLIG SKEGIAHMFL ALTDINDYVI
IPDPAYPVYR ATANIAGCNV YTMPLIAKEN YLPNLDNIYD EVKRKAKLLV VNYPNNPTGA
VADVEFFKKL IDFGKQNDIL IVNDAAYAEI LETGRKPVSI LQVEGAKDIS IEFGSLSKIF
SMTGWRVGFV VGNREAISKI VSVKSNFDSG QFIPIQKAAA YALDFTDIYV DFINDIYNER
RKIVVDVLRS KNLEVYDSKG TFYVWFKVPP NYNSEEFCSL ILERAHVLIT PGNAFGDRGE
GYARISLTSS TKEIKQAMDK INNINF
//
