ID A0A0S2HZ03_9BACT Unreviewed; 374 AA.
AC A0A0S2HZ03;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronate aminotransferase {ECO:0000313|EMBL:ALO15262.1};
DE EC=2.6.1.98 {ECO:0000313|EMBL:ALO15262.1};
GN Name=wbpE {ECO:0000313|EMBL:ALO15262.1};
GN ORFNames=L21SP5_01619 {ECO:0000313|EMBL:ALO15262.1};
OS Salinivirga cyanobacteriivorans.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Salinivirgaceae;
OC Salinivirga.
OX NCBI_TaxID=1307839 {ECO:0000313|EMBL:ALO15262.1, ECO:0000313|Proteomes:UP000064893};
RN [1] {ECO:0000313|EMBL:ALO15262.1, ECO:0000313|Proteomes:UP000064893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Spi-D4 {ECO:0000313|EMBL:ALO15262.1,
RC ECO:0000313|Proteomes:UP000064893};
RA Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT "Description and complete genome sequence of a novel strain predominating
RT in hypersaline microbial mats and representing a new family of the
RT Bacteriodetes phylum.";
RL Submitted (NOV-2015) 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; CP013118; ALO15262.1; -; Genomic_DNA.
DR RefSeq; WP_057952733.1; NZ_CP013118.1.
DR AlphaFoldDB; A0A0S2HZ03; -.
DR STRING; 1307839.L21SP5_01619; -.
DR KEGG; blq:L21SP5_01619; -.
DR PATRIC; fig|1307839.3.peg.1717; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000064893; 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; TRANSAMINASE; 1.
DR PANTHER; PTHR30244:SF42; UDP-2-ACETAMIDO-2-DEOXY-3-OXO-D-GLUCURONATE AMINOTRANSFERASE; 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:ALO15262.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000064893};
KW Transferase {ECO:0000313|EMBL:ALO15262.1}.
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 191
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 374 AA; 41753 MW; EE5A35A353D42AC6 CRC64;
MEQIQMVDLQ TQYKRLQKEI DESIQNVIEG AKFINGPAVK SFAANLADYL DVKHVIPCAN
GTDALQIALM SAGIQPGDEV ITPDFTFIAT VEVVALLGAK PVLADVNPED FTIDVNQLES
LITDKTKAIV PVHLFGQCAN MASIMNIARK HNLKVIEDTA QAIGSDYYIK DKPGKAGALG
DFGCTSFFPS KNLGCYGDGG ALYTNDDELA AIAKSITNHG STVKYHHDRI GVNSRLDAMQ
AAILKVKLKN LDDFNRRRQA AAIFYDHHLE EIPEIAIPVK RDASTHTYHQ YTIKVPKGEN
KKLQEYLKKH DIPSMIYYPI PLHKQAAFEQ WTDDRTFPVS DELAERVLSL PMHTELTKEQ
LTHICNTIKT YFHE
//