ID A0A0C1RG52_9ACTN Unreviewed; 393 AA.
AC A0A0C1RG52;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Aminotransferase class V domain-containing protein {ECO:0000259|Pfam:PF00266};
GN ORFNames=MB55_06595 {ECO:0000313|EMBL:KIE52877.1};
OS marine actinobacterium MedAcidi-G3.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1550402 {ECO:0000313|EMBL:KIE52877.1, ECO:0000313|Proteomes:UP000031370};
RN [1] {ECO:0000313|EMBL:KIE52877.1, ECO:0000313|Proteomes:UP000031370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mizuno C.M., Rodriguez-Valera F., Ghai R.;
RT "Novel reconstructed genomes of marine planktonic Acidimicrobiales.";
RL Submitted (SEP-2014) 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 -!- 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:KIE52877.1}.
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DR EMBL; JUEP01000010; KIE52877.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1RG52; -.
DR STRING; 1550402.MB55_06595; -.
DR Proteomes; UP000031370; Unassembled WGS sequence.
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50}.
FT DOMAIN 60..313
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 196
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 393 AA; 42226 MW; D8DA3BAC4AF6B8C0 CRC64;
MVSGRTFIQN PGPTNIPERI LRAMARPAVD FGTEEFGLLL GASLKTLNEY MANSGPLIGY
TSTGHGAWEA TVTNLFDVGA SVLLCDSGHF SHRWGEMCEA HGLDVQWFET GWRRGVDPDA
LREALSTESG SKVQGVLVAH TETSTGVTSD LAAMREVLND LNHSALLVVD SIASFGCAPL
AVDELGVDAC LAVSQKGLMM PVGLAFSGIS ERAVEVAYAN PRRRFYWDWR RRLEAEGYRS
FCGTPPIHHI FGLNEALSMF EEEGGIQAVT NRHRCLATAV RAAVEAWSSA GAIEFNAENE
HERSDSVTCV RVDPEYDADQ VIEIARAKYQ LTMGKGIGPL TGSAFRIGHL GDLNVPMVLG
ALGALETSLR ACRIPIGSGG LEAAAEKLSD LSS
//