ID A0A0Q5DZB5_9MICO Unreviewed; 957 AA.
AC A0A0Q5DZB5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:KQQ50572.1};
GN ORFNames=ASF68_16080 {ECO:0000313|EMBL:KQQ50572.1};
OS Plantibacter sp. Leaf314.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Plantibacter.
OX NCBI_TaxID=1736333 {ECO:0000313|EMBL:KQQ50572.1, ECO:0000313|Proteomes:UP000051200};
RN [1] {ECO:0000313|EMBL:KQQ50572.1, ECO:0000313|Proteomes:UP000051200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ50572.1,
RC ECO:0000313|Proteomes:UP000051200};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ50572.1, ECO:0000313|Proteomes:UP000051200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ50572.1,
RC ECO:0000313|Proteomes:UP000051200};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954}.
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:KQQ50572.1}.
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DR EMBL; LMOB01000002; KQQ50572.1; -; Genomic_DNA.
DR RefSeq; WP_056013338.1; NZ_LMOB01000002.1.
DR AlphaFoldDB; A0A0Q5DZB5; -.
DR STRING; 1736333.ASF68_16080; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000051200; 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; 3.90.1200.10; -; 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; IPR011009; Kinase-like_dom_sf.
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 SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KQQ50572.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000051200};
KW Transferase {ECO:0000313|EMBL:KQQ50572.1}.
SQ SEQUENCE 957 AA; 103029 MW; B1A5EB6F16D18BB3 CRC64;
MGTEYFDYFQ HVELPSPALP DDEVRRLFTA TFGVDVDVRS LGSQQDQNFR VFERGSSNPL
GVLKLSNPAF SETEIAMQDA ASALVGEREP ALRVPRAVVG PRGTMSAWWD TSQGRIHARV
IENLEGRTLM GSGHLSAAVV ERMGDLAARV SLALADFEHP AADRVLQWDL RHAGRVIDTL
LPLEPEADVR ATIRAAADDA LLALDRVADG LPIQAGHFDI TDDNVLRRSD EPLPDAVIDF
GDVVRSWRVG EIAVTVSSIL HHDGATITSG LPAIRAFHAR RPLDEHERTA LWPLVVLRGA
VLALSGRQQV RLDRENTYAS DALDREMRIL EVAASVPVQV MTTLIRDALG EPSRAGVEWL
GAPLLTFARA VAIDAGTLSE VNAEGAWMRE DTLAGAALAA LDDGADAAFL PPWRPVLTGA
PARTPSAPAT VPTGMGLWLA DATPVDRLGT VSAVRPGTIA VTGEHGTITV SGLPVTGVDV
LPARTPLFVQ LHHGPESPAP ERTTAALAPG WRSLLGDPGP AFGLAPQHPD DHDDVLDRRE
AVLAEVQEHY YAHPPQIERG WKEYLIDVDG RVYLDMVNNI ASIGHAHPRV ADAAYRQLRL
LNTNSRFHYR AIADYAERIA ATLPDELDTV FFVNSGSEAV DLAIRLAQAS TGRDDVVAMR
EAYHGWTYAS DAVSTSIADN PSALETRPDW VHTVAAANSY RGSHRGADAA KYAPEAAEAI
DALAAAGTPP AAFLCESYFG NAGGVALPDG YLRQVYAAVR RHGGVAIADE VQVGFGRLGE
WFWGFQQQDA VPDVVAVAKS IGAGQPIGAV ITSRAIADRY RTQGYFFSST GGSPLSSVVG
LAVLDVIRDE GLQENARRVG SHLKSRLETL RDQYPIIGTV HGSGLYLGLE FIRDQDTLEP
ATLETAAICD RLRELGVIMQ PTGDHLNVFK IKPPLCITEE SADYFVDAVA HVLATGW
//