ID R5JTN5_9CLOT Unreviewed; 364 AA.
AC R5JTN5;
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=BN743_01006 {ECO:0000313|EMBL:CCY57705.1};
OS Clostridium sp. CAG:632.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262830 {ECO:0000313|EMBL:CCY57705.1, ECO:0000313|Proteomes:UP000018242};
RN [1] {ECO:0000313|EMBL:CCY57705.1, ECO:0000313|Proteomes:UP000018242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:632 {ECO:0000313|Proteomes:UP000018242};
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|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:CCY57705.1}.
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DR EMBL; CAYL010000016; CCY57705.1; -; Genomic_DNA.
DR AlphaFoldDB; R5JTN5; -.
DR STRING; 1262830.BN743_01006; -.
DR Proteomes; UP000018242; 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; PTHR42885; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR42885:SF1; THREONINE-PHOSPHATE DECARBOXYLASE; 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:CCY57705.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018242};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:CCY57705.1}.
FT DOMAIN 30..359
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 364 AA; 41118 MW; 92C19401C1761FAA CRC64;
MLQPADQFHG SDLEKVEQLY GIKREDIRPF ASNVNPLGLS PILRSSLQEH IDVLTDYPDR
EYKELREAIH AYTGADAGHI LPGSGTTELI VTFIQAIRPK KTLVVEPTYS EYKRDLKAIK
SEIVNHVLSA ENDFRLDPAM LCEQIDESVD LVVLCNPNNP TSTCISISQI ETIARKCKEN
SAFLMIDETY VEFVKDISVI SAIPLVKKYN NIIVLRGVSK FFAAPGLRLG YACVSNEKLL
RYLWKHSNPW SISSLAAYAG TVMFTDREYM EQTRDLIAQE QSLICSALRA RGTIKVFQPA
TNFVLLQILK DGITSADVFE HCIRKGLMIR DCSNFMGLGP EYIRFCFLNP EDDDRLVNTL
LEIL
//