ID A0A1L9BT81_9RHOB Unreviewed; 393 AA.
AC A0A1L9BT81;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Aromatic amino acid aminotransferase {ECO:0000313|EMBL:OJH45496.1};
GN ORFNames=IE00_03935 {ECO:0000313|EMBL:OJH45496.1};
OS Paracoccus sp. SM22M-07.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1520813 {ECO:0000313|EMBL:OJH45496.1, ECO:0000313|Proteomes:UP000183790};
RN [1] {ECO:0000313|EMBL:OJH45496.1, ECO:0000313|Proteomes:UP000183790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM22M-07 {ECO:0000313|EMBL:OJH45496.1,
RC ECO:0000313|Proteomes:UP000183790};
RA Carlos C., Ottoboni L.;
RT "Draft sequencing and comparative genomics of Paracoccus sp. SM22M-07
RT isolated from coral mucus: Insights into bacteria-host interactions.";
RL Submitted (JUL-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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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:OJH45496.1}.
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DR EMBL; JPKW01000002; OJH45496.1; -; Genomic_DNA.
DR RefSeq; WP_072295770.1; NZ_JPKW01000002.1.
DR AlphaFoldDB; A0A1L9BT81; -.
DR STRING; 1520813.IE00_03935; -.
DR Proteomes; UP000183790; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR11879:SF22; ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:OJH45496.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000183790};
KW Transferase {ECO:0000313|EMBL:OJH45496.1}.
FT DOMAIN 28..388
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 393 AA; 42899 MW; D0346FAE867192A4 CRC64;
MLSNLKAQAP DKILMLIEEF KADTRQGKID LGVGVYKDPQ GVTPVMRAVK AAEQRIWESQ
TTKAYTSLAG EAEYRNSMAQ MVLGEVPADR LASVATVGGT GAIRQALELA RLANPDVTVF
VSNPTWPNHL SIMKFMGLPF VEYAYFDAET RGVDFEAMKA DISKAKKDDI VLLHGCCHNP
TGANLTLEQF EEVAAILEKS GAIPLIDLAY QGFGDGLDAD AAATRMIAQR LPQVLIAASC
SKNFGIYRER TGILMALTDN TATRDLTQGS LAFLNRQNYS FPPDHGARIV STILTDDALR
ADWAAELEDV RNTMLGLRTQ LASELRQLSG SDRFDFIEHH RGMFSRLGAT TEQVETLKRD
AGIYMVGDSR LNIAGLNTDT VPVLARAIIE AGI
//
