ID A0A1G7Y0Y2_9RHOO Unreviewed; 394 AA.
AC A0A1G7Y0Y2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Alanine-glyoxylate transaminase / serine-glyoxylate transaminase / serine-pyruvate transaminase {ECO:0000313|EMBL:SDG90047.1};
GN ORFNames=SAMN05660652_00857 {ECO:0000313|EMBL:SDG90047.1};
OS Propionivibrio dicarboxylicus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Propionivibrio.
OX NCBI_TaxID=83767 {ECO:0000313|EMBL:SDG90047.1, ECO:0000313|Proteomes:UP000198607};
RN [1] {ECO:0000313|EMBL:SDG90047.1, ECO:0000313|Proteomes:UP000198607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5885 {ECO:0000313|EMBL:SDG90047.1,
RC ECO:0000313|Proteomes:UP000198607};
RA de Groot N.N.;
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}.
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DR EMBL; FNCY01000002; SDG90047.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7Y0Y2; -.
DR STRING; 83767.SAMN05660652_00857; -.
DR OrthoDB; 9766472at2; -.
DR Proteomes; UP000198607; 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}; Pyruvate {ECO:0000313|EMBL:SDG90047.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198607}.
FT DOMAIN 36..303
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 206
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 394 AA; 42677 MW; 0D943A64F593AE32 CRC64;
MLRLDSHPSG QHFLHIPGPS PVPARILRAI SFQTIDHRGP EFGQLGLKVL EGIKQIFRTQ
HPVVIYPASG TGAWEAALVN TLSPGDLVLM YETGHFASLW RKLADRLGLQ TEFISFPGIE
GWRRGVDPER IAARLREDTQ HRIKAVCVVH NETSTGVVSD IAAVRRAIDA AGHPALLMVD
AVSGLGSAEY RHDDWGVDVT VAGSQKGLML PPGLGFNAIS PKALEASRLA RLPKAFWAWD
EYLDMNRNGY WPTTPATNLL YGLHEAIDMI LGEGLDNVLA RHQRLGAACR AAIDAWGLEN
LCLDPSQVSP VSTAVLLPEA YDADGLRRLI LERYNLSLGT GLGKVKGRVF RIGHLGDCNA
LTLLAALSGC EMGMRAFGVP LKASGVVAAQ ECLQ
//
