ID A8L2G0_FRASN Unreviewed; 489 AA.
AC A8L2G0;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ABW10353.1};
GN ORFNames=Franean1_0897 {ECO:0000313|EMBL:ABW10353.1};
OS Frankia sp. (strain EAN1pec).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW10353.1};
RN [1] {ECO:0000313|EMBL:ABW10353.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EAN1.pec {ECO:0000313|EMBL:ABW10353.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Rawnsley T., Niemann J., Benson D.R., Huang Y.,
RA Mastronunzio J., Bassi C.A., Tisa L.S., Richardson P.;
RT "Complete sequence of Frankia sp. EAN1pec.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP000820; ABW10353.1; -; Genomic_DNA.
DR AlphaFoldDB; A8L2G0; -.
DR STRING; 298653.Franean1_0897; -.
DR KEGG; fre:Franean1_0897; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_11; -.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
DR CDD; cd00610; OAT_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; IPR004632; 4NH2But_aminotransferase_bac.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00700; GABAtrnsam; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ABW10353.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ABW10353.1}.
FT REGION 468..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..489
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 51486 MW; 3A5B50C40BE6B4C7 CRC64;
MSETGQAQLP PRGGPGLPQV RRLVTAIPGP RSVELAKRRS QAVARGVGET LPVYIAAAGG
GVLVDVDGNS LIDFGSGIAV VSVGNAADAV VENVREQAGL FTHTCFMVTP YEGYVTVCEE
LARLTPGRHE KRSALFNSGA EAVENAVKIA RAHTGRSAVV AFAHAYHGRT NLTMALTAKS
MPYKHHFGPF APEIYRMPMA YPYRWPGGPA ACGEQAAAQV VETITTEIGA ENVAALVIEP
IQGEGGFIVP GTGFLTRLAE FCAQTGIVFV ADEVQTGFAR TGDMFACEHE GIVPDLIVTA
KGIAGGLPLA AVTGRAEIMD SPHVGGLGGT YGGNPVACAA ALGAIATIER GDLTARARRI
ERIAMPRLLA LRDRYPFIGD VRGRGAMLAL ELVADPTEGT PPNQPAPAPD RMVTVAAAAE
AHRRGLVLLT AGTWGNVLRL LPPLVIPDDL LLEGLDILDE AFADIARHRP RPRPRLQPQP
QPDSLPPTH
//
