ID Q2GA86_NOVAD Unreviewed; 415 AA.
AC Q2GA86;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:ABD25237.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:ABD25237.1};
GN OrderedLocusNames=Saro_0792 {ECO:0000313|EMBL:ABD25237.1};
OS Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS 56034 / CIP 105152 / NBRC 16084 / F199).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=279238 {ECO:0000313|EMBL:ABD25237.1, ECO:0000313|Proteomes:UP000009134};
RN [1] {ECO:0000313|Proteomes:UP000009134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084
RC / F199 {ECO:0000313|Proteomes:UP000009134};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL Submitted (JAN-2006) 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}.
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DR EMBL; CP000248; ABD25237.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2GA86; -.
DR STRING; 279238.Saro_0792; -.
DR KEGG; nar:Saro_0792; -.
DR eggNOG; COG1448; Bacteria.
DR HOGENOM; CLU_032440_0_1_5; -.
DR Proteomes; UP000009134; Chromosome.
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:ABD25237.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000009134};
KW Transferase {ECO:0000313|EMBL:ABD25237.1}.
FT DOMAIN 53..411
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 44436 MW; 1E71E4FA8BED5D8A CRC64;
MRGLPPPRSG GMEPPHFAPR NGRPRPMLEN LAAQPADALL ALIKLHNADP REDKIDLGVG
VYRTSEGATP VFKAIKAAEA KLLESQDSKA YLGPEGDMGF VHALIPYVFG KDFDRSKVEG
MQAPGGTGAV RLAIEVAKRS GVKRVWMGTP SWPNHAQIIA AAGMELKTFS HMTADGLADL
EALKTALAGA EAGDAVLLHG CCHNPTGVDY TEAQWDEIAP LLVERQVLPI LDLAYQGLGA
GMEADAYGLR KVLSLAPEAL VAYSCDKNFG LYRDRVGAFY AVTSDATALA NAMGNGATIA
RASWSMPPDH GAAAVRLILD DAELTAMWLA ELDEMRDRMR WVRDRLAAAQ HVGPINMAPL
GVQNGLFSML PLRADQILAI REKHGVYMAG SGRINIAGLT TGNIDKFVEA LRDVA
//
