ID A0A0G0ZTU3_9BACT Unreviewed; 424 AA.
AC A0A0G0ZTU3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Glutamine-scyllo-inositol transaminase {ECO:0000313|EMBL:KKS16433.1};
GN ORFNames=UU71_C0002G0010 {ECO:0000313|EMBL:KKS16433.1};
OS Parcubacteria group bacterium GW2011_GWB1_41_6.
OC Bacteria.
OX NCBI_TaxID=1618869 {ECO:0000313|EMBL:KKS16433.1, ECO:0000313|Proteomes:UP000034062};
RN [1] {ECO:0000313|EMBL:KKS16433.1, ECO:0000313|Proteomes:UP000034062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKS16433.1}.
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; LCBR01000002; KKS16433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0ZTU3; -.
DR STRING; 1618869.UU71_C0002G0010; -.
DR Proteomes; UP000034062; Unassembled WGS sequence.
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; 2.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}.
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 185
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 424 AA; 48819 MW; 0D6B257E48F63E7E CRC64;
MTIFSAPHPR FRIYTHLGSY TSLLIDLLFN RIIKGADVEK LEKAMAEKFR VSYAVAVPMA
RVGIYLTLKH LIKPGQGVIM SPYTVADVVN MVILAGGVPV FCDIEQKSCN IDSDKIERFI
DVKTGAVLVT HLHGIGADIY KILQICRSHN LPLVEDAAQS FGGYQNGKRL GTIGDVGIYS
FGMYKNINSW YGGAVVSENK VLIDKIKSEL NQYNYQSGCF ILKRMFKGLI TDFLTLPFVF
QSLTYWLFRY GFLNNIKWIN KRIEMELNIS RRDAVPPYYL VRLTPFQARL ALKQLDKIDR
ENEIRIQKAA LYHEGLRDIS GLILPPEGNI LSYIYTVFPV QYEDRKSLLK WLMFHKRDVA
AQHLKNCADL PSFSVFYRDC PITRKTANEV ILLPTYPRYP DTEIQKNIDV IRAYFKNRSI
WQQR
//
