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Database: UniProt
Entry: D5U4J1_BRAM5
LinkDB: D5U4J1_BRAM5
Original site: D5U4J1_BRAM5 
ID   D5U4J1_BRAM5            Unreviewed;       435 AA.
AC   D5U4J1;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:ADG70236.1};
GN   OrderedLocusNames=Bmur_0129 {ECO:0000313|EMBL:ADG70236.1};
OS   Brachyspira murdochii (strain ATCC 51284 / DSM 12563 / 56-150) (Serpulina
OS   murdochii).
OC   Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC   Brachyspira.
OX   NCBI_TaxID=526224 {ECO:0000313|EMBL:ADG70236.1, ECO:0000313|Proteomes:UP000001915};
RN   [1] {ECO:0000313|EMBL:ADG70236.1, ECO:0000313|Proteomes:UP000001915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51284 / DSM 12563 / 56-150
RC   {ECO:0000313|Proteomes:UP000001915};
RX   PubMed=21304710; DOI=10.4056/sigs.831993;
RA   Pati A., Sikorski J., Gronow S., Munk C., Lapidus A., Copeland A.,
RA   Glavina Del Tio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F.,
RA   Han C., Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Spring S.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Brachyspira murdochii type strain (56-150).";
RL   Stand. Genomic Sci. 2:260-269(2010).
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; CP001959; ADG70236.1; -; Genomic_DNA.
DR   RefSeq; WP_013112667.1; NC_014150.1.
DR   AlphaFoldDB; D5U4J1; -.
DR   STRING; 526224.Bmur_0129; -.
DR   KEGG; brm:Bmur_0129; -.
DR   eggNOG; COG0399; Bacteria.
DR   HOGENOM; CLU_033332_5_0_12; -.
DR   OrthoDB; 9810913at2; -.
DR   Proteomes; UP000001915; Chromosome.
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: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:ADG70236.1};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU004508};
KW   Transferase {ECO:0000313|EMBL:ADG70236.1}.
SQ   SEQUENCE   435 AA;  49342 MW;  9D7E58A1BB7E7DE7 CRC64;
     MDRNKLLEMV REYARKEYAP KEFVKGLSSV PVSGRVFDED DVAALVDSAL DFHLTTYRYN
     DEFEKGLKEF FGLKYALTCN SGSSANLIAV TSLTSHLLKD RALKAVDEVI TVAAGFPTTV
     NPILQNNLVP VFVDVELKTY NVNVEELEKA KSDKTKAVIL AHTLGNPFNI QKVREFCDKY
     NLWLIEDCCD ALGSTYNNKK VGTFGDIATL SFYPAHHITM GEGGAVLTDN PILKKAMESI
     RDWGRDCWCS PGCDDTCRQR FSQKIGDLPE GYDHKYTYSH LGYNLKITDM QAACGVAQLR
     KINEFIEKRK ENFKKIKNKL EKFSKYLILP KEQENSDPSW FGFLISVKEE APFTRNDIVK
     YLNDNKIGTR LLFAGNIIKQ PYMIGRNYRI VGELTNSDFI MNNTFWIGVY PGIDDSMIDY
     VELIIGEFIS NLGGK
//
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