ID A9M946_BRUC2 Unreviewed; 367 AA.
AC A9M946;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=L-glutamine:2-deoxy-scyllo-inosose aminotransferase {ECO:0000313|EMBL:ABX61610.1};
GN Name=rbmB {ECO:0000313|EMBL:ABX61610.1};
GN OrderedLocusNames=BCAN_A0533 {ECO:0000313|EMBL:ABX61610.1};
OS Brucella canis (strain ATCC 23365 / NCTC 10854).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=483179 {ECO:0000313|EMBL:ABX61610.1, ECO:0000313|Proteomes:UP000001385};
RN [1] {ECO:0000313|EMBL:ABX61610.1, ECO:0000313|Proteomes:UP000001385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23365 / NCTC 10854 {ECO:0000313|Proteomes:UP000001385};
RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA Bruce D., Detter C., Munk C., Brettin T.S.;
RT "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP000872; ABX61610.1; -; Genomic_DNA.
DR RefSeq; WP_004690643.1; NC_010103.1.
DR AlphaFoldDB; A9M946; -.
DR GeneID; 55590269; -.
DR KEGG; bcs:BCAN_A0533; -.
DR HOGENOM; CLU_033332_2_4_5; -.
DR PhylomeDB; A9M946; -.
DR Proteomes; UP000001385; Chromosome I.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 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:ABX61610.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Transferase {ECO:0000313|EMBL:ABX61610.1}.
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 182
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 367 AA; 40494 MW; 5EDA13CEECC6081D CRC64;
MDIPVYSPYL CGNFKKYVNE CLDTGWISSR GEFISRFEDA FAQYVDVPSA TSVANGTVAL
HLALDALGIG AGDEVIVPTF TYIASVNTIL QTGATPVYVD SLENTLQIDP EGVRLAITER
TKAVMVVHLY GHPCDMDSIR EICDEKSLLL VEDCAEGFGT KWKNSHVGTF GDVATFSFFG
NKTITTGEGG MVLARNPQVM EKCRHLKSQG TSPTREYWHD ALAYNYRMTN IQAAIGLSQI
EMADEILSLK ARTAASYASK LAGLPLRMHT PVGDVKHSYW MCSIVLDNSE HREPLRQHLR
ENGVDTRPFF PPAHRMPHSA STGSYPVADS LSARGLNLPS LPHITDVEIS FVCDLVRSYF
SNHSNHI
//
