ID A0A261QIP4_9BACI Unreviewed; 386 AA.
AC A0A261QIP4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Aminotransferase DegT {ECO:0000313|EMBL:OZI12705.1};
GN ORFNames=CEW92_04920 {ECO:0000313|EMBL:OZI12705.1};
OS Bacillaceae bacterium SAS-127.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=2015203 {ECO:0000313|EMBL:OZI12705.1, ECO:0000313|Proteomes:UP000217062};
RN [1] {ECO:0000313|EMBL:OZI12705.1, ECO:0000313|Proteomes:UP000217062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAS-127 {ECO:0000313|EMBL:OZI12705.1,
RC ECO:0000313|Proteomes:UP000217062};
RA Verma A., Pal Y., Krishnamurthi S.;
RT "Indiibacillus sp. (SAS-127) genome sequencing.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, 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:OZI12705.1}.
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; NKXN01000021; OZI12705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261QIP4; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000217062; 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; IPR026385; LegC-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR04181; NHT_00031; 1.
DR PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 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:OZI12705.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000217062};
KW Transferase {ECO:0000313|EMBL:OZI12705.1}.
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 217
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 386 AA; 42970 MW; 9471ECD3185E56A1 CRC64;
MIDQWQDVIA TIKSWALQKD FLPLHEPTFI GNEKKYVLDC IESGWVSSVG KYVDEFEQKL
AEFTGVKRAV AVVNGTSALH IALKLVGVQA DDEVIIPSLT FIATANAVTY KNAIPHFVDV
ERQTLGIDPQ KLRNYLADIA VIENGVCVNK ETQRVIRAIV PMHTFGHPVG IDELKKVADE
FHLALVEDAA ESLGSYYKGI HTGNFGQIAA VSFNGNKTIT TGGGGAILTN DDELADRAKH
LTTTAKVSHR WEYTHDEIGY NYRMPNINAA LGVAQLEQLP NYIEQKRQLA QKYKALFSSM
KGITLFEEPD QVKSNYWLQT IILDASIHDR DQVLELLNEH GIMSRPIWTP LHELTPFQSC
PKGDLTVTEQ LKKSVINVPS SPYLGS
//
