ID V1CQD1_9FIRM Unreviewed; 396 AA.
AC V1CQD1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=HMPREF9089_00365 {ECO:0000313|EMBL:ESE30950.1};
OS Eubacterium brachy ATCC 33089.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis.
OX NCBI_TaxID=1321814 {ECO:0000313|EMBL:ESE30950.1, ECO:0000313|Proteomes:UP000017536};
RN [1] {ECO:0000313|EMBL:ESE30950.1, ECO:0000313|Proteomes:UP000017536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33089 {ECO:0000313|EMBL:ESE30950.1,
RC ECO:0000313|Proteomes:UP000017536};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-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|ARBA:ARBA00007441,
CC 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:ESE30950.1}.
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DR EMBL; AXUD01000004; ESE30950.1; -; Genomic_DNA.
DR AlphaFoldDB; V1CQD1; -.
DR STRING; 1321814.HMPREF9089_00365; -.
DR PATRIC; fig|1321814.3.peg.338; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_9; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000017536; 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; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; 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:ESE30950.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017536};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ESE30950.1}.
FT DOMAIN 31..384
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 396 AA; 44397 MW; EE233B2AE32A5F7A CRC64;
MKLSKRVEEM QFSPIRKFNP IAQKAKDAGK KIYHLNIGQP DVETPSVFME AIRNFDQKVI
AYAESGGLPV LQDAIIEYFK KYNMEYIRDE IIVTTGGSEA LTMAFLAIIN DGDEVLIPEP
FYTNYHTFAT SAGGKVVPIT TKAEDGYHYA QREQIERAIT SKTKAICCIS PGNPTGTVLT
LDEIKLIGEI AKKHDLYIIA DEVYREFAYD GRDVTSFGME PGITDRVIII DSVSKRFSAC
GARIGCIVSK NKEFMEAVMK IAQGRLCTST VDQIGAAALY KLPRSYYDKV KAEYCARRDV
VFEELQKIPG VVCQKPGGSF YITAKLPVDN VEDFLMFLLE DFDDNGETVM FAPAEGFYAT
EGLGRDELRI AYVLNKQDMR RGVELIRLGL EAYNKK
//
