ID Q1ILE9_KORVE Unreviewed; 394 AA.
AC Q1ILE9;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:ABF42301.1};
GN OrderedLocusNames=Acid345_3300 {ECO:0000313|EMBL:ABF42301.1};
OS Koribacter versatilis (strain Ellin345).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Koribacter.
OX NCBI_TaxID=204669 {ECO:0000313|EMBL:ABF42301.1, ECO:0000313|Proteomes:UP000002432};
RN [1] {ECO:0000313|EMBL:ABF42301.1, ECO:0000313|Proteomes:UP000002432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin345 {ECO:0000313|EMBL:ABF42301.1,
RC ECO:0000313|Proteomes:UP000002432};
RX PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(2009).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP000360; ABF42301.1; -; Genomic_DNA.
DR RefSeq; WP_011524100.1; NC_008009.1.
DR AlphaFoldDB; Q1ILE9; -.
DR STRING; 204669.Acid345_3300; -.
DR EnsemblBacteria; ABF42301; ABF42301; Acid345_3300.
DR KEGG; aba:Acid345_3300; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_0_3_0; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000002432; Chromosome.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ABF42301.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000002432};
KW Transferase {ECO:0000313|EMBL:ABF42301.1}.
FT ACT_SITE 192
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 192
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 394 AA; 43729 MW; 4B7BEB0FD23FA170 CRC64;
MKAETKLAEP QLQVPFHSAD VGEAEAQAAA DVIRSGWLTM GARTIEFERQ FAEYVGAKHA
IAVNSCTAAL HLALEAIHLQ QGDEVLVPTT TFTATGEVVT YFGAKPVLVD VEPDTLLMSV
ADAAARITPK TKAIIPVHYG GQPCDMDEIL ALAAKHNIHV IEDAAHSLPA SYKGRPVGCI
SEITAFSFYA TKTLSTGEGG MITTGNDDLA ARMRIMRLHG IGRDAWKRYS AEGSWYYEVL
DAGFKYNLTD IAAAIGLVQL GKCDDMNVRR AAVVQRYNDA FASMNELQVP TTKPDRQSAW
HLYPLRFHLD RIKIDRKEVI CQLKDRGIGT SVHFIPLHLH PYYQSAYGYR RGDLPAAERE
YERYVSLPLF PGMTYEQIDH VIHSVKQIVK ANRR
//
