ID A0A1I3U5D5_9CELL Unreviewed; 402 AA.
AC A0A1I3U5D5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=(S)-ureidoglycine-glyoxylate aminotransferase {ECO:0000313|EMBL:SFJ77066.1};
GN ORFNames=SAMN05216467_0890 {ECO:0000313|EMBL:SFJ77066.1};
OS Cellulomonas sp. KH9.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1855324 {ECO:0000313|EMBL:SFJ77066.1, ECO:0000313|Proteomes:UP000199404};
RN [1] {ECO:0000313|Proteomes:UP000199404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH9 {ECO:0000313|Proteomes:UP000199404};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOSE01000001; SFJ77066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3U5D5; -.
DR STRING; 1855324.SAMN05216467_0890; -.
DR Proteomes; UP000199404; 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:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 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:SFJ77066.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000199404};
KW Transferase {ECO:0000313|EMBL:SFJ77066.1}.
FT DOMAIN 39..342
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 194
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 402 AA; 42717 MW; 5220F363DAE57FAF CRC64;
MTLNPPHRLL MGPGPINADP RVLRAMSAPL VGQFDPVMTG YMNATQELYR GVFRTGNEAT
LLVDGTARAA IEAAVVSLVE PGDRVVVPVF GRFGHLLVEI ARRAGATVET VEAPWGEVVD
PQRVADAVRR HRPRLVAVVH GDTSTTMRQP LAEIGAVCAE HDALLYVDAT ASLGGNELHT
DAWGLDVVTA GLQKCLGGPS GSAPTTLSDR ARDAVRARRH VEEGLRTDED EPRGAVIRSN
YLDLAQILDY WGPRRLNHHT EATSMLYAAH ECARVLLEEG LDDAVERHRV AGAAMLAGVR
GLGLEVFGDT AHRMHNVVAV EVPDGVVADA VRAAMLDDFA IEIGTSFGPL HGRVWRIGTM
GVNARKDAVL TTLAALEHVL RGLGVAVAAG GGVDAAQAVY AA
//