ID E7GDA3_9FIRM Unreviewed; 371 AA.
AC E7GDA3;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=HMPREF9488_02746 {ECO:0000313|EMBL:EFW03954.1};
OS Coprobacillus cateniformis.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Coprobacillus.
OX NCBI_TaxID=100884 {ECO:0000313|EMBL:EFW03954.1, ECO:0000313|Proteomes:UP000003157};
RN [1] {ECO:0000313|EMBL:EFW03954.1, ECO:0000313|Proteomes:UP000003157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=29_1 {ECO:0000313|EMBL:EFW03954.1,
RC ECO:0000313|Proteomes:UP000003157};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Sibley C.D.,
RA White A., Strauss J., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J.,
RA Yandava C., Nusbaum C., Birren B.;
RT "The Genome Sequence of Coprobacillus sp. strain 29_1.";
RL Submitted (DEC-2010) 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:EFW03954.1}.
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DR EMBL; ADKX01000041; EFW03954.1; -; Genomic_DNA.
DR RefSeq; WP_008789833.1; NZ_WSNW01000001.1.
DR AlphaFoldDB; E7GDA3; -.
DR STRING; 100884.GCA_000269565_00399; -.
DR GeneID; 78228312; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_4_9; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000003157; 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; PTHR43510; AMINOTRANSFERASE FUNCTION, HYPOTHETICAL (EUROFUNG); 1.
DR PANTHER; PTHR43510:SF1; AMINOTRANSFERASE FUNCTION, HYPOTHETICAL (EUROFUNG); 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 Reference proteome {ECO:0000313|Proteomes:UP000003157};
KW Transferase {ECO:0000256|RuleBase:RU000481}.
FT DOMAIN 36..349
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 371 AA; 42492 MW; FD3FD953082A0B8D CRC64;
MKIAEFEVET WMTDHENHCR YNLTETCVSS LSLNDLQKYV QEDISKTIMS MTLDYGPIVG
SSRLKQAILS LYETGTVENI TIAHGAINAN ELVMISLLEP GDHIVSLFPS YQQMYDFPKS
LGCEVSLIHL SEEKKWMPTI EDFKQCMRNN TKMICLNSPN NPTGTTLPLS FMKELITLAK
DFDCYILCDE IYRGVNTITQ TMSPSFSDYY EKAIVTQSLS KVFSFPGLRL GWIKGSKEVV
HTIDMRRDYH IISSGPMDDY LACLVLENKE HIIKRSLYIC DESKKILKSW LEQEHLVSCV
IPDEGTVCFL KYEVDMPSIE FCEKLQAETG IFFVPGSAFG VENHLRFGLT HLNEIKEGLP
LFSQWLRQFD K
//