ID A0A061LXF7_9MICO Unreviewed; 431 AA.
AC A0A061LXF7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:EYT52491.1};
GN ORFNames=H490_0112640 {ECO:0000313|EMBL:EYT52491.1};
OS Leucobacter sp. UCD-THU.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1292023 {ECO:0000313|EMBL:EYT52491.1, ECO:0000313|Proteomes:UP000026917};
RN [1] {ECO:0000313|EMBL:EYT52491.1, ECO:0000313|Proteomes:UP000026917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-THU {ECO:0000313|EMBL:EYT52491.1,
RC ECO:0000313|Proteomes:UP000026917};
RX PubMed=23792744; DOI=10.1128/genomeA.00325-13;
RA Holland-Moritz H.E., Bevans D.R., Lang J.M., Darling A.E., Eisen J.A.,
RA Coil D.A.;
RT "Draft Genome Sequence of Leucobacter sp. Strain UCD-THU (Phylum
RT Actinobacteria).";
RL Genome Announc. 1:S69-S82(2013).
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC 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:EYT52491.1}.
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DR EMBL; APJM01000024; EYT52491.1; -; Genomic_DNA.
DR RefSeq; WP_017882502.1; NZ_APJM01000024.1.
DR AlphaFoldDB; A0A061LXF7; -.
DR STRING; 1292023.H490_0112640; -.
DR HOGENOM; CLU_016922_8_0_11; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000026917; 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; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
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:EYT52491.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000026917};
KW Transferase {ECO:0000313|EMBL:EYT52491.1}.
SQ SEQUENCE 431 AA; 44908 MW; 1CBDFC4728C0B5C6 CRC64;
MDLLEDGGGG ASRLGASLGA RLAQADPGDR DVAGVRLDEA VHRAQNGFEN YLDAYNNVPA
IGHSHPAVTA AVGAQIATLN THTRYLTDPV VDYAERIVAK FPAPLERVTF ACTGSEAVDL
AIRTARYGTG NRGLIVTEHA YHGTTHAAAQ VSPSLGPNNP VGDHVALIPS IDTARAPAHE
VATRLLDSVS AAIADLNERG HGVAAVILDS VFSSDGVQVE PAGFLAPVVQ AVHDAGGLYI
ADEVQPGFGR TGEWWGFQRH GIVPDLVVLG KPMGNGVPIS AVVGTVAAQE RFGSEVRYFN
TFGGNPVSIA AATAVLDVIE QDGLVEHAAR VGGELLSGLQ SLMGDYERIT DVRGAGLFLA
ADLGSRDAGL SPDPELAARV VNALRDEGVL ISASGPAAAT LKIRPPLPFT SNHADLLLEK
LELVLRRETR A
//
