(data stored in ACNUC7421 zone)

SWISSPROT: Q47T78_THEFY

ID   Q47T78_THEFY            Unreviewed;       421 AA.
AC   Q47T78;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 89.
DE   RecName: Full=Diaminobutyrate--2-oxoglutarate transaminase {ECO:0000256|RuleBase:RU365034};
DE            EC=2.6.1.76 {ECO:0000256|RuleBase:RU365034};
DE   AltName: Full=DABA aminotransferase {ECO:0000256|RuleBase:RU365034};
GN   OrderedLocusNames=Tfu_0301 {ECO:0000313|EMBL:AAZ54339.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54339.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Catalyzes reversively the conversion of L-aspartate
CC       beta-semialdehyde (ASA) to L-2,4-diaminobutyrate (DABA) by
CC       transamination with L-glutamate. {ECO:0000256|RuleBase:RU365034}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-2,4-diaminobutanoate = L-aspartate 4-
CC         semialdehyde + L-glutamate; Xref=Rhea:RHEA:11160,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58761,
CC         ChEBI:CHEBI:537519; EC=2.6.1.76;
CC         Evidence={ECO:0000256|RuleBase:RU365034};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU365034};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis;
CC       L-ectoine from L-aspartate 4-semialdehyde: step 1/3.
CC       {ECO:0000256|RuleBase:RU365034}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP000088; AAZ54339.1; -; Genomic_DNA.
DR   RefSeq; WP_011290748.1; NC_007333.1.
DR   STRING; 269800.Tfu_0301; -.
DR   EnsemblBacteria; AAZ54339; AAZ54339; Tfu_0301.
DR   KEGG; tfu:Tfu_0301; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K00836; -.
DR   OMA; NLMPGVQ; -.
DR   OrthoDB; 386839at2; -.
DR   BioCyc; TFUS269800:G1G4Q-303-MONOMER; -.
DR   UniPathway; UPA00067; UER00121.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0045303; F:diaminobutyrate-2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047307; F:diaminobutyrate-pyruvate transaminase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019491; P:ectoine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR004637; Dat.
DR   InterPro; IPR012773; Ectoine_EctB.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR43552; PTHR43552; 1.
DR   PANTHER; PTHR43552:SF2; PTHR43552:SF2; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 3.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00709; dat; 1.
DR   TIGRFAMs; TIGR02407; ectoine_ectB; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47T78.
DR   SWISS-2DPAGE; Q47T78.
KW   Aminotransferase {ECO:0000256|RuleBase:RU365034,
KW   ECO:0000313|EMBL:AAZ54339.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Transferase {ECO:0000256|RuleBase:RU365034,
KW   ECO:0000313|EMBL:AAZ54339.1}.
SQ   SEQUENCE   421 AA;  45677 MW;  8D9B07C1FD9F37CD CRC64;
     METFSRLESE VRSYCRGWPT LFTRARGSRV YDHTGRGYLD FFAGAGALNY GHNNPTLKTA
     LLDYLGSDSI VHSLDAATTA KRDFLDTFEE VILKPRGLDY KVQFPGPTGT NAVEAALKLA
     RKVTGRETVI SFTNSFHGMT LGALAVTGNS MKRGGAGVPL NHTVTMPFDN YMDGQVPDFL
     WLRSLLEDSG SGLDRPAAVI VETVQGEGGI NVARADWLRG LAELCREHEL LLIVDDIQMG
     CGRTGPFFSF EEAGIVPDIV TLSKSISGYG LPMALTLFKR ELDVWEPGEH NGTFRGFNPA
     FLTATVALNT YWRDDSLERE TLAKGQLITE RLEAIAAEHA EAGASVRGRG MACGLVLPGE
     GDARRVCAEA FERGLLMETS GPEDEVAKLL PPLTTSVAEM EEGLDILAES VRAAVRTPQP
     A
//

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