ID F2NCE1_DESAR Unreviewed; 391 AA.
AC F2NCE1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Glutamine--scyllo-inositol transaminase {ECO:0000313|EMBL:AEB09005.1};
DE EC=2.6.1.50 {ECO:0000313|EMBL:AEB09005.1};
GN OrderedLocusNames=Desac_1141 {ECO:0000313|EMBL:AEB09005.1};
OS Desulfobacca acetoxidans (strain ATCC 700848 / DSM 11109 / ASRB2).
OC Bacteria; Thermodesulfobacteriota; Desulfobaccia; Desulfobaccales;
OC Desulfobaccaceae; Desulfobacca.
OX NCBI_TaxID=880072 {ECO:0000313|EMBL:AEB09005.1, ECO:0000313|Proteomes:UP000000483};
RN [1] {ECO:0000313|EMBL:AEB09005.1, ECO:0000313|Proteomes:UP000000483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700848 / DSM 11109 / ASRB2
RC {ECO:0000313|Proteomes:UP000000483};
RX PubMed=21886866;
RA Goker M., Teshima H., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Huntemann M., Liolios K., Ivanova N., Pagani I., Mavromatis K.,
RA Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Brambilla E.M., Rohde M., Spring S., Detter J.C., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of the acetate-degrading sulfate reducer
RT Desulfobacca acetoxidans type strain (ASRB2).";
RL Stand. Genomic Sci. 4:393-401(2011).
RN [2] {ECO:0000313|Proteomes:UP000000483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700848 / DSM 11109 / ASRB2
RC {ECO:0000313|Proteomes:UP000000483};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA Teshima H., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schueler E.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Desulfobacca acetoxidans DSM 11109.";
RL Submitted (MAR-2011) 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; CP002629; AEB09005.1; -; Genomic_DNA.
DR RefSeq; WP_013706117.1; NC_015388.1.
DR AlphaFoldDB; F2NCE1; -.
DR STRING; 880072.Desac_1141; -.
DR KEGG; dao:Desac_1141; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_0_3_7; -.
DR OrthoDB; 9766188at2; -.
DR Proteomes; UP000000483; 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:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 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:AEB09005.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000000483};
KW Transferase {ECO:0000313|EMBL:AEB09005.1}.
FT ACT_SITE 189
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 189
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 391 AA; 43099 MW; C5EF21A34F2697EE CRC64;
MNPWKVPLAD VTLGPEEIAA VTEVLQSGWL SMGPRTQEFE ERFATFLGIK HAFAVANCTA
ALHLAGEVVG LQTGDEVLCP ALTFVATANA ILYTGAQPVF VDINGPHDLN ISPGDAAAKI
TPRTRALMVV HYAGYPCDMD SLVELAKQHN LKIIEDCAHA PGAVYQSAAG PQKAGTIGNI
GCFSFFSNKN MTTGEGGMLV TNDDELAAKI KVARSHGMTT LTWDRHKGHS FSYDVIARGY
NFRLDEIRAA LGIVQLERLV AGNARRRELT LAYQEKLREL EQLELPFLRA PVGSTHHIFP
VLLNKEINRF ELMTALAQAG IQTSIHYPPV HRFTHYRHLL GENFDHRLPL TEDAAARELT
LPLYPALSST QLEIVTETIR NFLTSGRFHR I
//
