ID R7GD05_9FIRM Unreviewed; 388 AA.
AC R7GD05;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=BN631_00447 {ECO:0000313|EMBL:CDE23812.1};
OS Amedibacillus dolichus CAG:375.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Amedibacillus.
OX NCBI_TaxID=1263076 {ECO:0000313|EMBL:CDE23812.1, ECO:0000313|Proteomes:UP000018093};
RN [1] {ECO:0000313|EMBL:CDE23812.1, ECO:0000313|Proteomes:UP000018093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:375 {ECO:0000313|Proteomes:UP000018093};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDE23812.1}.
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DR EMBL; CBIN010000299; CDE23812.1; -; Genomic_DNA.
DR RefSeq; WP_004800800.1; NZ_FR898536.1.
DR AlphaFoldDB; R7GD05; -.
DR GeneID; 83059545; -.
DR Proteomes; UP000018093; 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:SF5; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383; 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:CDE23812.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018093};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:CDE23812.1}.
FT DOMAIN 30..379
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 388 AA; 43791 MW; 0C35E31C4D4BE964 CRC64;
MYEQYLSDKV KQIKPSGIRK YFDMASEMEG VISLGVGEPD FTTPWHICEA AIYSIEEGRT
HYTANQGLLE LREAICDYQY RRFHLTYDPI KNVIVTVGGS EAIDIAMRAI VNPGDEVILM
EPSYVAYTPS VELQGGIPVY IKLSHEDEFK LTAEKLEAAI SDKTKAILLN FPSNPTGGVM
SKEDYEKLVP IIKKHNLIVL SDEIYAELTY DTDFCSLASF DEIKDQVIII SGFSKAYAMT
GWRLGYTLAN ETFTQAMNKI HQYIIMSAPT AAQYGAIEAM RHGDVHVQEM KESYQARRNF
ITRGFNRLGL PTHLPQGAFY IFPDIRSTGL TSDEFCEQLL LDQKVACVPG TAFGDAGEGF
IRISYAYSIE HIKEALERIE KFLTKLRK
//
