ID I4WQ66_9GAMM Unreviewed; 379 AA.
AC I4WQ66;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Class V aminotransferase {ECO:0000313|EMBL:EIM01608.1};
GN ORFNames=UU5_01572 {ECO:0000313|EMBL:EIM01608.1};
OS Rhodanobacter sp. 115.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1162282 {ECO:0000313|EMBL:EIM01608.1, ECO:0000313|Proteomes:UP000004557};
RN [1] {ECO:0000313|EMBL:EIM01608.1, ECO:0000313|Proteomes:UP000004557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=115 {ECO:0000313|EMBL:EIM01608.1,
RC ECO:0000313|Proteomes:UP000004557};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236}.
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:EIM01608.1}.
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DR EMBL; AJXS01000038; EIM01608.1; -; Genomic_DNA.
DR RefSeq; WP_008208267.1; NZ_AJXS01000038.1.
DR AlphaFoldDB; I4WQ66; -.
DR PATRIC; fig|1162282.3.peg.305; -.
DR OrthoDB; 9766472at2; -.
DR Proteomes; UP000004557; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR PANTHER; PTHR21152:SF24; SERINE--PYRUVATE AMINOTRANSFERASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EIM01608.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Transferase {ECO:0000313|EMBL:EIM01608.1}.
FT DOMAIN 23..335
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 198
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 379 AA; 40983 MW; C09E833C370FB011 CRC64;
MHAPQSPGVD PNGLQEYSVV FTDRALNHMS QRFQQVMHDL SRNLKTVYHA HAVALVPGGG
TTGMESVARQ FAHGKNVLII RNGWFSYRWS QIFEVGRIPS HTTVLKARPT GTAHQAPFAP
PPIDDVIASI AEHKPDLVFA PHVETSSGML LPDDYLQRVA TAVHAHGGMF VLDCIASGTL
WVDMEKVGVD VLLSAPQKTW SASPCAALVM LSAEAEARLK ATQSSSFTLD LAKWRAVMTA
YENGGHAYHS TMPTDALVTL RDAMDETVAM GLEHARNAQL ELGRKVRALL AHRNLPSVAT
EGFQAPGVVV SYTDDDAIHN GSAFAKRGLQ IAAGTPLACD EPADFKTFRL GLFGIDKLRD
VDGTAQRLDD ALNDMQAGT
//