ID E0IE62_9BACL Unreviewed; 440 AA.
AC E0IE62;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Glutamine--scyllo-inositol transaminase {ECO:0000313|EMBL:EFM09416.1};
DE EC=2.6.1.50 {ECO:0000313|EMBL:EFM09416.1};
GN ORFNames=PaecuDRAFT_3953 {ECO:0000313|EMBL:EFM09416.1};
OS Paenibacillus curdlanolyticus YK9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM09416.1, ECO:0000313|Proteomes:UP000005387};
RN [1] {ECO:0000313|EMBL:EFM09416.1, ECO:0000313|Proteomes:UP000005387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YK9 {ECO:0000313|EMBL:EFM09416.1,
RC ECO:0000313|Proteomes:UP000005387};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Anderson I.J.,
RA Johnson E., Loganathan U., Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RT "The draft genome of Paenibacillus curdlanolyticus YK9.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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; AEDD01000011; EFM09416.1; -; Genomic_DNA.
DR RefSeq; WP_006039938.1; NZ_AEDD01000011.1.
DR AlphaFoldDB; E0IE62; -.
DR STRING; 717606.PaecuDRAFT_3953; -.
DR eggNOG; COG0399; Bacteria.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000005387; Unassembled WGS sequence.
DR GO; GO:0047310; F:glutamine-scyllo-inositol transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0080100; F:L-glutamine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
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:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EFM09416.1};
KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000005387};
KW Transferase {ECO:0000313|EMBL:EFM09416.1}.
SQ SEQUENCE 440 AA; 48866 MW; 5E1B3499C59F7467 CRC64;
MKTDFIRKPL QLPDEEWIKS PLALDGGPSI IPEDVRKTNF PIITKEDVIQ LFVSIQQDGE
SVVEEFKEAY RNYVGANYAI ATSSGTSSLH LALVGVGVQP GDEVIVPAFT FIATAQAVVA
AKAIPIFVDI DPVTYCLDAT KVEEAITHKT KAIMPVHVHG LPADLSALRQ LADKHGLRLV
EDASHAHSAS IDGQVAGSIG DSAGQSLMAD KNFPVGGEGG IAFFREKEDY ERALAFLDAS
GIDYRMSWIA AAFGLSQLDR LPYYDAIRAR NAAYLTDALK ETKLFSGPFV PEGYKHSYNM
YRVKLHPERL GLGDLDDYRV KHAVEQLIHA EGVFAREWQN VPIPGHLPFK NRRGFGNGYP
FSLSDREDFG YDLNRFPVTL NMLRSTLTIC RELRTPIEYE RIQAYALAFK KVDANPHKIR
ELVEQGGDVK IVYERDARLG
//