ID A0A419A3H7_9RHOB Unreviewed; 375 AA.
AC A0A419A3H7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Alanine--glyoxylate aminotransferase family protein {ECO:0000313|EMBL:RJL08109.1};
GN ORFNames=D3P05_16650 {ECO:0000313|EMBL:RJL08109.1};
OS Paracoccus siganidrum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1276757 {ECO:0000313|EMBL:RJL08109.1, ECO:0000313|Proteomes:UP000283587};
RN [1] {ECO:0000313|Proteomes:UP000283587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26381 {ECO:0000313|Proteomes:UP000283587};
RA Jurado V., Gutierrez-Patricio S., Gonzalez-Pimentel J.L., Miller A.Z.,
RA Laiz L., Saiz-Jimenez C.;
RT "Paracoccus onubensis nov. sp. a moderate halophilic bacterium isolated
RT from Gruta de las Maravillas (Aracena, Spain).";
RL Submitted (SEP-2018) 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:RJL08109.1}.
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DR EMBL; QZEW01000079; RJL08109.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A419A3H7; -.
DR OrthoDB; 9766472at2; -.
DR Proteomes; UP000283587; 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:RJL08109.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000283587};
KW Transferase {ECO:0000313|EMBL:RJL08109.1}.
FT DOMAIN 22..284
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 375 AA; 40320 MW; 84AFE94E6D6A7CB8 CRC64;
MPGLRPEIDP DGLQEFSVVF TDRSLNHMSQ AFQQVMRDLS ATLREVYGAD QVAIVPGGGS
YAMEAVARQF ARGRHALIVR NGWFSYRWSQ ILETGGLPSE TTVAMARPFG NEPQPAFAPP
PIDEVVATIR DQRPDLVFAP HVETAAGLIL PDDYITALSG AAHEVGALMV LDCIASGAVW
VDMRALGVDV LISAPQKGWS ASPSAGLVML SERAAARLQE TESDSFALDL KKWRAIMAAY
EDGGHAYHAT MPTDALRGLR DAMEETRQMG FQAAREAQWR LGDGVRALLA EKGIRPVAAE
GFGAPGVVVS YTSDPEIRSG RKFAAEGLQI AAGVPLAVNE GADFSTFRIG LFGLDKLKDV
EGTIGRLKTA IDKLL
//
