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Database: UniProt
Entry: A0A0K8JF04_9FIRM
LinkDB: A0A0K8JF04_9FIRM
Original site: A0A0K8JF04_9FIRM 
ID   A0A0K8JF04_9FIRM        Unreviewed;       388 AA.
AC   A0A0K8JF04;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   Name=yugH {ECO:0000313|EMBL:CUH96187.1};
GN   ORFNames=P22_2276 {ECO:0000313|EMBL:CUH96187.1};
OS   Propionispora sp. 2/2-37.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Propionispora.
OX   NCBI_TaxID=1677858 {ECO:0000313|EMBL:CUH96187.1, ECO:0000313|Proteomes:UP000041641};
RN   [1] {ECO:0000313|EMBL:CUH96187.1, ECO:0000313|Proteomes:UP000041641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2/2 {ECO:0000313|EMBL:CUH96187.1};
RA   Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA   Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA   Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL   Submitted (SEP-2015) 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|RuleBase:RU000481}.
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DR   EMBL; CYSP01000009; CUH96187.1; -; Genomic_DNA.
DR   RefSeq; WP_054260344.1; NZ_CYSP01000009.1.
DR   AlphaFoldDB; A0A0K8JF04; -.
DR   STRING; 1677858.P22_2276; -.
DR   OrthoDB; 9802328at2; -.
DR   Proteomes; UP000041641; 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:SF3; ASPARTATE AMINOTRANSFERASE-RELATED; 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:CUH96187.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000041641};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:CUH96187.1}.
FT   DOMAIN          31..380
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   388 AA;  43114 MW;  469F44B7698BE67C CRC64;
     MSWSERISPR VQSIPPSGIR RFFDIVSEME DVISLGVGEP DFVTPWHIRD SCVDGLHRGY
     TSYTSNYGLL ELRKEIALLK SNDFGISYDP RNEILVTVGV SEALDLAMRT LLCPGDEVLI
     PEPCYVSYKA CVTLAGGIPV TVPTSIATEF CVTAEQLEKY VTPCTKVLII GYPNNPTGAV
     MPHREMEKIA KFVKKYDLVV ISDEIYGKLT YDGQHTCFAS LPDMKDRTIL LDGFSKAYAM
     TGWRIGYAMS NPEFIAAMTK IHQFTMLCAP ITAQIAALEA LRRGDKAVQE MVSEYNHRRR
     LMLEGFRSAG LSCFEPKGAF YIFPSIKETG LSSLAFAEEL LKAEKVALVP GDAFGTCGEG
     YVRCSYATSS ENLTLALERI ARFVKKYL
//
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