ID A0A3N1B1H6_9ACTN Unreviewed; 458 AA.
AC A0A3N1B1H6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ROO62620.1};
GN ORFNames=EDC02_4601 {ECO:0000313|EMBL:ROO62620.1};
OS Micromonospora sp. Llam0.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2485143 {ECO:0000313|EMBL:ROO62620.1, ECO:0000313|Proteomes:UP000275308};
RN [1] {ECO:0000313|EMBL:ROO62620.1, ECO:0000313|Proteomes:UP000275308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Llam0 {ECO:0000313|EMBL:ROO62620.1,
RC ECO:0000313|Proteomes:UP000275308};
RA D'Agostino P.;
RT "Genome mining of underrepresented organisms for secondary metabolites.";
RL Submitted (NOV-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 -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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:ROO62620.1}.
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DR EMBL; RJJY01000001; ROO62620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1B1H6; -.
DR OrthoDB; 4510254at2; -.
DR Proteomes; UP000275308; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; 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 PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 3.
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:ROO62620.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000275308};
KW Transferase {ECO:0000313|EMBL:ROO62620.1}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 48260 MW; C6773049887F69EB CRC64;
MTTTPDWFDP DRPQPHLVTE LPGPQAREVL ARDRAVTSPS LPRAYAIAPR RGHGAVVEDV
DGNLFLDFNA GIAVTSTGHC HPSVVEAVQQ QAATLLHYSA SDFYLPLYGQ MCQALAETAP
MDGPVRVFLT NSGAEAVEGA LKLSRYATGR QYVISFYGSF HGRTYGAMTL TGSKSKYHKG
FGPLLPGVLH APYAPASLDF IEEVLFEHQV DPSEVAAIFV EPIQGEGGFI VPPAGWLARL
RRICDQHGIL LVADEVQCGM GRTGRMWAIE HTGVQPDILI SAKGIASGLP LGAFLARSEL
MERWGPGAHG STYGGSPVPC AAGLATLRVI QDEGLLDNAT AQGEFLLAGL RELQQAYPRL
LVDVRGVGLM IGVEFPTGEI AGQVQQAAFT RGLLVLEAGV NAVRMSPPLV ITRAQAQTGL
RLFGAAVAEV AADLQATGNG KVEAGGAVEA GGSVAVPG
//
