ID U5MX61_CLOSA Unreviewed; 367 AA.
AC U5MX61;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Glutamine--scyllo-inositol transaminase {ECO:0000313|EMBL:AGX45128.1};
DE EC=2.6.1.50 {ECO:0000313|EMBL:AGX45128.1};
GN ORFNames=CLSA_c41680 {ECO:0000313|EMBL:AGX45128.1};
OS Clostridium saccharobutylicum DSM 13864.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1345695 {ECO:0000313|EMBL:AGX45128.1, ECO:0000313|Proteomes:UP000017118};
RN [1] {ECO:0000313|EMBL:AGX45128.1, ECO:0000313|Proteomes:UP000017118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13864 {ECO:0000313|EMBL:AGX45128.1};
RX PubMed=24285650;
RA Poehlein A., Hartwich K., Krabben P., Ehrenreich A., Liebl W., Durre P.,
RA Gottschalk G., Daniel R.;
RT "Complete Genome Sequence of the Solvent Producer Clostridium
RT saccharobutylicum NCP262 (DSM 13864).";
RL Genome Announc. 1:e00997-13(2013).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP006721; AGX45128.1; -; Genomic_DNA.
DR RefSeq; WP_022750019.1; NZ_AYXL01000227.1.
DR AlphaFoldDB; U5MX61; -.
DR GeneID; 55476453; -.
DR KEGG; csb:CLSA_c41680; -.
DR PATRIC; fig|1345695.10.peg.2059; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_2_4_9; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000017118; Chromosome.
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 PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:AGX45128.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000017118};
KW Transferase {ECO:0000313|EMBL:AGX45128.1}.
FT ACT_SITE 180
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 180
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 367 AA; 41387 MW; 132AB8A486F82195 CRC64;
MIKLASPDIG QEELDEIKKV FDSKYLVQGD KVEEFENQLK EYLNAKYCFA VSSGTAALHL
ALLAIGIKAN DEVIVPDFTF PATANVVEIV GATTKFVDIK LDSLCIDTDK IENAITDKTK
AIIPVHEFGQ PADMDKIVAI AKKYNLKVIE DAACALGAEY KGKKVGTIGD IGCFSLHPRK
AITTGEGGIV VTNNSKLAES IRILRNHGLN YKNGKIRFVQ AGLNYRMTNI QGAIGTVQMK
KLELINERRI EVAKKYNNLL KNVKFVTLPE EKSYEKHVWQ TYHILLDKRI DRDKLISKLK
DKGIETNFGA YSVHEEPYYK EKYGYENCQF YNSIYAHKHG MALPMHNNIC SKEIIYIVSE
LEKILNE
//
