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Database: UniProt/TrEMBL
Entry: A0A127NSI3_9CORY
LinkDB: A0A127NSI3_9CORY
Original site: A0A127NSI3_9CORY 
ID   A0A127NSI3_9CORY        Unreviewed;       442 AA.
AC   A0A127NSI3;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   25-OCT-2017, entry version 11.
DE   SubName: Full=4-aminobutyrate transaminase {ECO:0000313|EMBL:AMO88474.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:AMO88474.1};
GN   Name=gabT {ECO:0000313|EMBL:AMO88474.1};
GN   ORFNames=WM42_0732 {ECO:0000313|EMBL:AMO88474.1};
OS   Corynebacterium simulans.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=146827 {ECO:0000313|EMBL:AMO88474.1, ECO:0000313|Proteomes:UP000074804};
RN   [1] {ECO:0000313|EMBL:AMO88474.1, ECO:0000313|Proteomes:UP000074804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PES1 {ECO:0000313|EMBL:AMO88474.1,
RC   ECO:0000313|Proteomes:UP000074804};
RX   PubMed=26861018;
RG   NISC Comparative Sequencing Program;
RA   Tsai Y.C., Conlan S., Deming C., Segre J.A., Kong H.H., Korlach J.,
RA   Oh J.;
RT   "Resolving the Complexity of Human Skin Metagenomes Using Single-
RT   Molecule Sequencing.";
RL   MBio 7:e01948-15(2016).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP014634; AMO88474.1; -; Genomic_DNA.
DR   RefSeq; WP_062035700.1; NZ_CP014634.1.
DR   EnsemblBacteria; AMO88474; AMO88474; WM42_0732.
DR   GeneID; 29537023; -.
DR   KEGG; csp:WM42_0732; -.
DR   PATRIC; fig|146827.5.peg.711; -.
DR   KO; K07250; -.
DR   Proteomes; UP000074804; 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; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00700; GABAtrnsam; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:AMO88474.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000074804};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000313|EMBL:AMO88474.1}.
SQ   SEQUENCE   442 AA;  47368 MW;  AE09413B839A8D58 CRC64;
     MQELEYRIEQ TRHLAQEVPG PASAALDERR KNAIPAGMAP SLPGYVVDAD GGILADADGN
     RFIDLASGIA VTSAGASNPA VVKAVQEAVA HFTHTSFTIS PYESYVEVAE KLNEVTPGDH
     PKKTALFNSG AEAVENAVKI ARNYTGKRGV VVMDRAFHGR TNLTMAMTAK QSPYKNGFGP
     FAPEIYRAPM SYPLRDQLSG EEAAKKTLTM IEQEVGAANL ACVVVEPIQG EGGFVVPAEG
     YLPAIQKWCN DNDVVFIVDE IQAGMMRTGT WFASDHEGIV PDLVTIAKGI ASGMPLSAVT
     GRAEIMDAPQ PGGLGGTYTG NPVSCAAALA TLKEFEEKDF GARALNLEKI AREELEPILG
     DERVAEFRGR GAMLALEFVT ADGEPDSELV HKIADAAKAE GVLILTCGLD HNVIRFLPSL
     AIPEDLWREA LQVVVKQFNE YK
//
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