ID A0LW96_ACIC1 Unreviewed; 387 AA.
AC A0LW96;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:ABK53706.1};
GN OrderedLocusNames=Acel_1934 {ECO:0000313|EMBL:ABK53706.1};
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC Acidothermus.
OX NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK53706.1, ECO:0000313|Proteomes:UP000008221};
RN [1] {ECO:0000313|EMBL:ABK53706.1, ECO:0000313|Proteomes:UP000008221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B
RC {ECO:0000313|Proteomes:UP000008221};
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(2009).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP000481; ABK53706.1; -; Genomic_DNA.
DR RefSeq; WP_011720769.1; NC_008578.1.
DR AlphaFoldDB; A0LW96; -.
DR STRING; 351607.Acel_1934; -.
DR KEGG; ace:Acel_1934; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_6_0_11; -.
DR InParanoid; A0LW96; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000008221; 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:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 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:ABK53706.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000008221};
KW Transferase {ECO:0000313|EMBL:ABK53706.1}.
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 186
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 387 AA; 41947 MW; 2338B86DDE08541D CRC64;
MPIPLVDLTW QHSVIEPQVL PTLLDVMRRG AFIGGAAVEE FEADFARYCE VTHCVGVANG
TDAIEIALRA LHIGPGDEVI VPTNTFVATV EAVLRAGAIP RLVDCDDEYL LIDPRGVEAA
ISPRTRAVIA VHLYGQVAPM RDLAKIAEKH NLALIEDAAQ CQGARLDGRR AGGLGHIAAT
SFYPGKNLGA YGDGGAVLTD DEGLARYARR LANHGSARKY HHPDIGFNSR LDALQAVILR
EKLRRLDDWN ALRQEIAVYY SERLAEIDEV RVPTVRPGNE HVWHLYVIRI PRRDSVLAAL
NRAGIGAAVH YPIPVHLQPG YVGLGYRAGD FPVAERAATQ ILSLPIFPGM TTSQCDVVID
TLREALTVGE TSPGDGSPLA HETGAVR
//
