ID D5V6D6_ARCNC Unreviewed; 362 AA.
AC D5V6D6;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Glutamine--scyllo-inositol transaminase {ECO:0000313|EMBL:ADG94206.1};
DE EC=2.6.1.50 {ECO:0000313|EMBL:ADG94206.1};
GN OrderedLocusNames=Arnit_2557 {ECO:0000313|EMBL:ADG94206.1};
OS Arcobacter nitrofigilis (strain ATCC 33309 / DSM 7299 / CCUG 15893 / LMG
OS 7604 / NCTC 12251 / CI) (Campylobacter nitrofigilis).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Arcobacteraceae; Arcobacter.
OX NCBI_TaxID=572480 {ECO:0000313|EMBL:ADG94206.1, ECO:0000313|Proteomes:UP000000939};
RN [1] {ECO:0000313|EMBL:ADG94206.1, ECO:0000313|Proteomes:UP000000939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33309 / DSM 7299 / CCUG 15893 / LMG 7604 / NCTC 12251 / CI
RC {ECO:0000313|Proteomes:UP000000939};
RX PubMed=21304714; DOI=10.4056/sigs.912121;
RA Pati A., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA Lucas S., Tice H., Cheng J.F., Han C., Chertkov O., Bruce D., Tapia R.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Arcobacter nitrofigilis type strain (CI).";
RL Stand. Genomic Sci. 2:300-308(2010).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP001999; ADG94206.1; -; Genomic_DNA.
DR RefSeq; WP_013136351.1; NC_014166.1.
DR AlphaFoldDB; D5V6D6; -.
DR STRING; 572480.Arnit_2557; -.
DR KEGG; ant:Arnit_2557; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_6_0_7; -.
DR OrthoDB; 9766188at2; -.
DR Proteomes; UP000000939; 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:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 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:ADG94206.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000000939};
KW Transferase {ECO:0000313|EMBL:ADG94206.1}.
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 362 AA; 40720 MW; 48EA67E65A393964 CRC64;
MILCANPKEQ YLTHKTEIQN AINKVLESGW YILGQEVKLF ENEFSNFVGT KYTISVASGT
DALFLALKAL NIGTGDEVIT VSHTATATVS AIKATGATPI MVDIEKEYFT IDIEEVKKRV
SNKTKAIIAV HIYGQPCDMD ALIKISNENN IDIIEDCAQA SGASYKGKEL GSIGTLGCFS
FFPTKNLGAI GDGGAITTNC EKLYNKLLKL RQYGWDENRD SEFSGYNSRL DELQAAILRV
KLKYLKQDTK KRNDIAKLYY EALKNSSLIL PKVRDNCYHS FHLFVVRLKN RNQLKEYLKS
KNILAMIHYE KPVHLQEAFT INHDLNCTEN IAGEILSLPM YPELSEKDIK YISTKCLEVK
ES
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