ID A0A074M4M2_9BACL Unreviewed; 445 AA.
AC A0A074M4M2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:KEO80957.1};
GN ORFNames=EL26_23445 {ECO:0000313|EMBL:KEO80957.1};
OS Tumebacillus flagellatus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Tumebacillus.
OX NCBI_TaxID=1157490 {ECO:0000313|EMBL:KEO80957.1, ECO:0000313|Proteomes:UP000027931};
RN [1] {ECO:0000313|EMBL:KEO80957.1, ECO:0000313|Proteomes:UP000027931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GST4 {ECO:0000313|EMBL:KEO80957.1,
RC ECO:0000313|Proteomes:UP000027931};
RX PubMed=23435245; DOI=10.1099/ijs.0.045351-0;
RA Wang Q., Xie N., Qin Y., Shen N., Zhu J., Mi H., Huang R.;
RT "Tumebacillus flagellatus sp. nov., an alpha-amylase/pullulanase-producing
RT bacterium isolated from cassava wastewater.";
RL Int. J. Syst. Evol. Microbiol. 63:3138-3142(2013).
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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:KEO80957.1}.
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DR EMBL; JMIR01000053; KEO80957.1; -; Genomic_DNA.
DR RefSeq; WP_038094506.1; NZ_JMIR01000053.1.
DR AlphaFoldDB; A0A074M4M2; -.
DR STRING; 1157490.EL26_23445; -.
DR eggNOG; COG0161; Bacteria.
DR OrthoDB; 9807885at2; -.
DR Proteomes; UP000027931; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KEO80957.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000027931};
KW Transferase {ECO:0000313|EMBL:KEO80957.1}.
SQ SEQUENCE 445 AA; 49110 MW; E1F11545C9F7445A CRC64;
MSEKETLLAA DRAHMWHHMS PYNPNPMIVT ESQGSWITDI DGNRYLDGMS GLWCVNIGYG
RQELADAAYE QMKALAYFPL TQSHVPAIRL SQKISEWLEG EHRVFFSNSG SEANEVAFKM
ARQYHAQRGE PGRYKFISRY RAYHGNTMGA LAATGQAVRK QSYEPLAPGF KHVPPPYCYR
CPYGKTYGSC SLECAAAIDE MINWEGAETV AAVIMEPTIT GGGVIVPPPE YLPKVREICD
KHGVLLIIDE VICGAGRSGR KFGHQNFNVQ PDIVTMAKGI TSGYLPLSAT AVRAEIADVF
LEPGVNQHFR HLNTFGGNPA ACALALRNLE LIESEGLIQR VEQLGAELRA KLTPLESHPH
VGDIRSFGFV CGIEVVEDRA TKEASAPDRV LRIIAECKKR GLIIGRNGDT IPGYNNILTL
APPFSTTDED LEFLVNVLTE VFDLI
//
