ID G8S5H5_ACTS5 Unreviewed; 446 AA.
AC G8S5H5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=4-aminobutyrate aminotransferase / (S)-3-amino-2-methylpropionate transaminase {ECO:0000313|EMBL:AEV84975.1};
DE EC=2.6.1.22 {ECO:0000313|EMBL:AEV84975.1};
GN Name=gabT {ECO:0000313|EMBL:AEV84975.1};
GN OrderedLocusNames=ACPL_4080 {ECO:0000313|EMBL:AEV84975.1};
OS Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV84975.1, ECO:0000313|Proteomes:UP000005440};
RN [1] {ECO:0000313|Proteomes:UP000005440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC {ECO:0000313|Proteomes:UP000005440};
RA Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA Wehmeier U.F., Stoye J., Puehler A.;
RT "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT SE50/110.";
RL Submitted (DEC-2011) 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; CP003170; AEV84975.1; -; Genomic_DNA.
DR AlphaFoldDB; G8S5H5; -.
DR STRING; 134676.ACPL_4080; -.
DR KEGG; ase:ACPL_4080; -.
DR PATRIC; fig|134676.3.peg.3995; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_11; -.
DR Proteomes; UP000005440; Chromosome.
DR GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:UniProtKB-EC.
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 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:AEV84975.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000005440};
KW Transferase {ECO:0000313|EMBL:AEV84975.1}.
SQ SEQUENCE 446 AA; 46928 MW; 8D5F688177F6B0D6 CRC64;
MNRLCRVSLE QKRRLVTALP GPRSQELMER KLAAVAGGVG TTMPVFAARA GGGIVVDVDG
NHLIDLGSGI AVTTVGAGAP RVVAAVTEQV AAFTHTCFMV TPYDGYVAVA EALNRVTPGD
HEKRSVLFNS GAEAVENAVK IARAHTGRDA VVVFDHAYHG RTNLTMAMTA KSMPYKHGFG
PFAPEVYRAP GSYPYRDAGV DGRAAAARAI DQIEKQIGAD NLAALVIEPI QGEGGFIEPA
AGFLPALAAW CRANGVVFVA DEVQTGFART GDMFACDREG VVPDLIVTAK GIAGGLPLSA
VTGRAEIMDA PHAGGLGGTY GGNPIACAAA LAAIETIEQD GLLARAREIE TRVTGRLHDI
RDKDDRLGDI RGRGAMIAVE LVRAGGREAD PRLARDVARY AHQRGVIVLT CGTYGNVLRF
LPPLSITNEL LDDAFDVLAA AFQEIR
//
