ID A0A0L6U2S7_9FIRM Unreviewed; 395 AA.
AC A0A0L6U2S7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Aminotransferase DegT {ECO:0000313|EMBL:KNZ42657.1};
GN ORFNames=AKG39_05835 {ECO:0000313|EMBL:KNZ42657.1};
OS Acetobacterium bakii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=52689 {ECO:0000313|EMBL:KNZ42657.1, ECO:0000313|Proteomes:UP000036873};
RN [1] {ECO:0000313|Proteomes:UP000036873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8239 {ECO:0000313|Proteomes:UP000036873};
RA Song Y., Hwang S., Cho B.-K.;
RT "Draft genome sequence of Acetobacterium bakii DSM 8293, a potential
RT psychrophilic chemical producer through syngas fermentation.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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:KNZ42657.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGYO01000011; KNZ42657.1; -; Genomic_DNA.
DR RefSeq; WP_050739424.1; NZ_UOGO01000001.1.
DR AlphaFoldDB; A0A0L6U2S7; -.
DR STRING; 52689.AKG39_05835; -.
DR PATRIC; fig|52689.4.peg.258; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000036873; Unassembled WGS sequence.
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; IPR020026; PseC.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR03588; PseC; 1.
DR PANTHER; PTHR30244:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 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:KNZ42657.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000036873};
KW Transferase {ECO:0000313|EMBL:KNZ42657.1}.
FT ACT_SITE 194
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 194
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 395 AA; 44348 MW; 3617C98C29A9050E CRC64;
MKIAFKGGTP ARDIFIPYGK QYIDEHDIEA VTKVLKSPYL TTGPKVEEFE KKLCGITGAK
YAIALSSGTS ALHAACHAAG IQQGDEVITT PMTFAASANC ILYCGGTPVF ADIDAGTWNI
KPEEIEKNVT SKTKAVIAVD FTGQAVQLDE IRDICKRYNL ILIEDAAHAI GTKYNGIPVG
NISDLTTFSF HPVKTITCGE GGAVLTNNEE YYKKIMLFRS HAITREIDEI SQHPFNGYNE
QIGLGYNYRM TDMQAALGIS QLDKLWIFSN RRSEIVKKYN EAFSEIPQLT IQQEIQESDT
TRHLYIIRIK SSLLKVNRNE IYKALNAENI GLQVHYIPVY YHPYYQSLGY NKGICPIAEK
LYEEIITIPL YFSLTDDDVQ DVIKGIKKVI NYYKC
//
