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Database: UniProt
Entry: E0IE62_9BACL
LinkDB: E0IE62_9BACL
Original site: E0IE62_9BACL 
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}.
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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
//
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