ID A0A099F1K2_9RHOB Unreviewed; 382 AA.
AC A0A099F1K2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Aspartate aminotransferase {ECO:0000313|EMBL:SFA55745.1};
DE SubName: Full=Class V aminotransferase {ECO:0000313|EMBL:KGJ04148.1};
GN ORFNames=IT41_11610 {ECO:0000313|EMBL:KGJ04148.1}, SAMN04487972_11428
GN {ECO:0000313|EMBL:SFA55745.1};
OS Paracoccus halophilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=376733 {ECO:0000313|EMBL:KGJ04148.1, ECO:0000313|Proteomes:UP000029846};
RN [1] {ECO:0000313|EMBL:KGJ04148.1, ECO:0000313|Proteomes:UP000029846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14014 {ECO:0000313|EMBL:KGJ04148.1,
RC ECO:0000313|Proteomes:UP000029846};
RA McGinnis J.M., Wolfgang W.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGJ04148.1, ECO:0000313|Proteomes:UP000029846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14014 {ECO:0000313|EMBL:KGJ04148.1,
RC ECO:0000313|Proteomes:UP000029846};
RA Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT York State patients.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SFA55745.1, ECO:0000313|Proteomes:UP000182312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6117 {ECO:0000313|EMBL:SFA55745.1,
RC ECO:0000313|Proteomes:UP000182312};
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; JRKN01000014; KGJ04148.1; -; Genomic_DNA.
DR EMBL; FOJO01000014; SFA55745.1; -; Genomic_DNA.
DR RefSeq; WP_036741280.1; NZ_JRKN01000014.1.
DR AlphaFoldDB; A0A099F1K2; -.
DR STRING; 376733.SAMN04487972_11428; -.
DR eggNOG; COG0075; Bacteria.
DR OrthoDB; 9766472at2; -.
DR Proteomes; UP000029846; Unassembled WGS sequence.
DR Proteomes; UP000182312; 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:KGJ04148.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000029846};
KW Transferase {ECO:0000313|EMBL:KGJ04148.1}.
FT DOMAIN 22..325
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 382 AA; 40698 MW; 57178D82BFAEB1DF CRC64;
MPGLLPDLDP EGLQEFSVVF TDRSLNHMSR RFQAAMRDIS ATLREVYRAE AVALVPGGGT
CAMEAVARQF GRDAHALIVR NGFFSYRWSQ IFEAGGFTRE TTVMMARQSG NEPTAPFAPA
PVDEVVARIR AARPDAVFAP HVETAAGMIL PDAYIRALAD AAHEVGAIMV LDCIASGAIW
VDMAATGVDV LISAPQKGWS ASPSAGMVML SARGAARLAD TVSDSFVLDL KKWRAIMQAY
EEGGHAYHAT LPTDALIGLR DAMDETRAMG FEAAREAQWR LGDAVRAELA RRGFRSVAAE
GFAAPGVVVV HTDDPELQSG RKFLAAGYQI AAGVPLQVGE GEGFRSFRIG LFGLDKLQDV
DGTLARLIAG FDAALSGGDM PG
//
