ID A0A0U4C795_9ACTN Unreviewed; 445 AA.
AC A0A0U4C795;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ALX03822.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:ALX03822.1};
GN ORFNames=AERYTH_03430 {ECO:0000313|EMBL:ALX03822.1};
OS Aeromicrobium erythreum.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=2041 {ECO:0000313|EMBL:ALX03822.1, ECO:0000313|Proteomes:UP000067689};
RN [1] {ECO:0000313|EMBL:ALX03822.1, ECO:0000313|Proteomes:UP000067689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR18 {ECO:0000313|EMBL:ALX03822.1,
RC ECO:0000313|Proteomes:UP000067689};
RX PubMed=1883712;
RA Miller E.S., Woese C.R., Brenner S.;
RT "Description of the erythromycin-producing bacterium Arthrobacter sp.
RT strain NRRL B-3381 as Aeromicrobium erythreum gen. nov., sp. nov.";
RL Int. J. Syst. Bacteriol. 41:363-368(1991).
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; CP011502; ALX03822.1; -; Genomic_DNA.
DR RefSeq; WP_067854664.1; NZ_CP011502.1.
DR AlphaFoldDB; A0A0U4C795; -.
DR STRING; 2041.AERYTH_03430; -.
DR KEGG; aer:AERYTH_03430; -.
DR PATRIC; fig|2041.4.peg.718; -.
DR OrthoDB; 4510254at2; -.
DR Proteomes; UP000067689; Chromosome.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
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:ALX03822.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000067689};
KW Transferase {ECO:0000313|EMBL:ALX03822.1}.
SQ SEQUENCE 445 AA; 45774 MW; 711C87E18C82E27C CRC64;
MSVPQRRHLT TPLPGPRSQE LMARKSAAVA GGVGTTMPVF AAQAGGGVVV DVDGNSLIDL
GSGIAVTTVG NSAPRVVAAV QEQVAAFTHT CFMVTPYEGY VAVAEALNRL TPGDHEKRTA
LFNSGAEAVE NAVKIARAHT GRQAVVVFDH AYHGRTNLTM AMTAKSMPYK QGFGPFASEV
YRAPLSYPFR DGGLDGATAA ARALDVVEKQ VGAVNVAAVV VEPIQGEGGF IEPAPGFLPA
LAAWCRENGV VFVADEVQTG FARTGDLFAC DREGVVPDLV VTAKGIAGGL PLSAVTGRAE
IMDAPHAGGL GGTYGGNPLA CAAALAAIET VEQDGLVERA RAVEAFLKER LHALQARDAR
VGDVRGRGAM IAVELVRPGT TDPDPDLARA VSAAAHAEGV IVLTCGTYGN VLRLLPPLAI
DDTLLGEGLD VLEAAFASTL VGAAQ
//