ID R6HX88_9FIRM Unreviewed; 420 AA.
AC R6HX88;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:CDB41640.1};
GN ORFNames=BN517_01661 {ECO:0000313|EMBL:CDB41640.1};
OS Ruminococcus sp. CAG:177.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1262952 {ECO:0000313|EMBL:CDB41640.1, ECO:0000313|Proteomes:UP000018315};
RN [1] {ECO:0000313|EMBL:CDB41640.1, ECO:0000313|Proteomes:UP000018315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:177 {ECO:0000313|Proteomes:UP000018315};
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 -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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:CDB41640.1}.
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DR EMBL; CBDQ010000051; CDB41640.1; -; Genomic_DNA.
DR AlphaFoldDB; R6HX88; -.
DR STRING; 1262952.BN517_01661; -.
DR Proteomes; UP000018315; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CDB41640.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000018315};
KW Transferase {ECO:0000313|EMBL:CDB41640.1}.
SQ SEQUENCE 420 AA; 46586 MW; 08A638E3B3F9BCA7 CRC64;
MSFKINDYTK SREMFERAEK VIPSGVYGHL GPAEGCFIPV SAFPLFGDRA QGSYFWDVDG
NKFIDYMCAY GPNVLGYNDP DVDAAALEQA KKCNCTTSPS YKAVEFAELL VDTVNCADWA
FFAKNGNDVT TAAIMTARAH THRKKIIFIN GFYHGISPWT QKVDYPGVLE EDVANNIYID
WNDIPALERA IAENEGEIAA FISTPYLHGN FFDNQLPADG YWQKVRELCT KNGIVLIVDD
VRAGFRLDLA GSDHFYGFEA DLICFCKALA NGWNVSALCG KEFLKSSISS LSYTGSYWLS
AIPFAAGIAC INKMKKLNTP ALFREKGLKV GEGLKAAAAN NGFHLVVSGE PSLFYLRLAD
DDSLMLHQEW VAEMVKRGIF ITSHHNHFLN ASLTDEDIAH TVDVAEDAFN TLRKNHPELA
//
