ID R5N2V3_9FIRM Unreviewed; 405 AA.
AC R5N2V3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN ORFNames=BN519_01224 {ECO:0000313|EMBL:CCY91921.1};
OS Eubacterium sp. CAG:180.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1262882 {ECO:0000313|EMBL:CCY91921.1, ECO:0000313|Proteomes:UP000018411};
RN [1] {ECO:0000313|EMBL:CCY91921.1, ECO:0000313|Proteomes:UP000018411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:180 {ECO:0000313|Proteomes:UP000018411};
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-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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:CCY91921.1}.
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DR EMBL; CAZC010000053; CCY91921.1; -; Genomic_DNA.
DR AlphaFoldDB; R5N2V3; -.
DR STRING; 1262882.BN519_01224; -.
DR Proteomes; UP000018411; 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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43488; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR PANTHER; PTHR43488:SF2; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CCY91921.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018411};
KW Transferase {ECO:0000313|EMBL:CCY91921.1}.
FT DOMAIN 34..394
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 405 AA; 45438 MW; E6786B337550C9AC CRC64;
MRKFSKSHKL DHVCYDIRGP VLEKASEMES AGTKILKLNI GNPAPFNFSA PDEIIHDMIY
TLRDAEGYSD SKGIFSARKS IMQYSQLKNL PNVGINDIYT GNGVSELITM SMQGLLDNGD
EILVPAPDYP LWTAAVTLAG GNAVHYICDE QNEWNPDIDD IKKKITDRTK GIVIINPNNP
TGALYSEEIL KEIVAVARSH QLIIFSDEIY DRLVMDSLKH ISIASLAPDI PCITFNGLSK
SHRIAGFRCG WMCISGNKAP IKDYIEGLNL LSSMRLCSNV PAQEIIQTAL GGYQSIDELL
LPGGRIYEQR EAVWKALNSI DGVSAMKPKA AFYIFPKIDS KKYNIKNDEQ MVYDFLVSKK
ILLVQGSAFN YPTPDHVRIV YLPTVKQLNK ACEEFEYFLK HYKQK
//