ID A0A1V3ITC9_9PAST Unreviewed; 386 AA.
AC A0A1V3ITC9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=UDP-4-amino-4, 6-dideoxy-N-acetyl-beta-L-altrosamine transaminase {ECO:0000313|EMBL:OOF45497.1};
GN ORFNames=BKK52_12545 {ECO:0000313|EMBL:OOF45497.1};
OS Rodentibacter trehalosifermentans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Rodentibacter.
OX NCBI_TaxID=1908263 {ECO:0000313|EMBL:OOF45497.1, ECO:0000313|Proteomes:UP000189161};
RN [1] {ECO:0000313|EMBL:OOF45497.1, ECO:0000313|Proteomes:UP000189161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1987082031 {ECO:0000313|EMBL:OOF45497.1,
RC ECO:0000313|Proteomes:UP000189161};
RA Christensen H.;
RT "Rodentibacter gen. nov. and new species.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OOF45497.1}.
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DR EMBL; MLHL01000095; OOF45497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3ITC9; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000189161; Unassembled WGS sequence.
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; IPR020026; PseC.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR03588; PseC; 1.
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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000189161}.
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 188
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 386 AA; 43678 MW; 815B9066BA037247 CRC64;
MIPYGKQDIN QDDIDAVIQV LQSDFLTQGP KVPAFENSIK EYCHVKYALA VNSATSALHI
ACLALGLGKG DWLWTTPITF VASANCGLYC GASIDFVDVD PKTYNISVKK LAEKLKIAKQ
ENRLPKVVVP VHLTGQICEM DKIRELSKEY GFYVIEDASH AIGGKYKGQA VGNCEYSDIT
VFSFHPVKII TTAEGGLCTT NNPELAEKME LFRSHGITRN PAKMTKEPDG AWYYQQINLG
YNYRMTELQA ALGVSQMSRL DEFIKARHIL AKRYDELLES LPVITPWQLP DSYSGLHLYV
IRLKLDQIQK THKQVFDELR SRNIGVNLHY IPVYSQPYYQ QFGFKSKDFP EAEKYYQEAI
SLPMYSSLAF EQQDIVIAAL KDILCD
//
