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Database: UniProt
Entry: H6NB34_9BACL
LinkDB: H6NB34_9BACL
Original site: H6NB34_9BACL 
ID   H6NB34_9BACL            Unreviewed;       441 AA.
AC   H6NB34;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Diaminobutyrate--2-oxoglutarate transaminase {ECO:0000256|ARBA:ARBA00014798, ECO:0000256|RuleBase:RU365034};
DE            EC=2.6.1.76 {ECO:0000256|ARBA:ARBA00013155, ECO:0000256|RuleBase:RU365034};
DE   AltName: Full=DABA aminotransferase {ECO:0000256|RuleBase:RU365034};
GN   ORFNames=PM3016_4533 {ECO:0000313|EMBL:AFC31289.1};
OS   Paenibacillus mucilaginosus 3016.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1116391 {ECO:0000313|EMBL:AFC31289.1, ECO:0000313|Proteomes:UP000007523};
RN   [1] {ECO:0000313|EMBL:AFC31289.1, ECO:0000313|Proteomes:UP000007523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3016 {ECO:0000313|EMBL:AFC31289.1,
RC   ECO:0000313|Proteomes:UP000007523};
RX   PubMed=22535950; DOI=10.1128/JB.00323-12;
RA   Ma M., Wang Z., Li L., Jiang X., Guan D., Cao F., Chen H., Wang X.,
RA   Shen D., Du B., Li J.;
RT   "Complete Genome Sequence of Paenibacillus mucilaginosus 3016, a Bacterium
RT   Functional as Microbial Fertilizer.";
RL   J. Bacteriol. 194:2777-2778(2012).
CC   -!- FUNCTION: Catalyzes reversively the conversion of L-aspartate beta-
CC       semialdehyde (ASA) to L-2,4-diaminobutyrate (DABA) by transamination
CC       with L-glutamate. {ECO:0000256|ARBA:ARBA00002189,
CC       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, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58761, ChEBI:CHEBI:537519;
CC         EC=2.6.1.76; Evidence={ECO:0000256|ARBA:ARBA00001487,
CC         ECO:0000256|RuleBase:RU365034};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU365034};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC       ectoine from L-aspartate 4-semialdehyde: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004946, 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; CP003235; AFC31289.1; -; Genomic_DNA.
DR   AlphaFoldDB; H6NB34; -.
DR   STRING; 1116391.PM3016_4533; -.
DR   KEGG; pmq:PM3016_4533; -.
DR   HOGENOM; CLU_016922_10_0_9; -.
DR   UniPathway; UPA00067; UER00121.
DR   Proteomes; UP000007523; 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; 3.90.1150.10; 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; IPR004637; Dat.
DR   InterPro; IPR012773; Ectoine_EctB.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00709; dat; 1.
DR   NCBIfam; TIGR02407; ectoine_ectB; 1.
DR   PANTHER; PTHR43552; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43552:SF2; DIAMINOBUTYRATE--2-OXOGLUTARATE TRANSAMINASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 3.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU365034,
KW   ECO:0000313|EMBL:AFC31289.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007523};
KW   Transferase {ECO:0000256|RuleBase:RU365034, ECO:0000313|EMBL:AFC31289.1}.
SQ   SEQUENCE   441 AA;  48952 MW;  0D7E695F86DF9E37 CRC64;
     MKQILSQFRW RMKRVSIFEK LESNVRSYCR SFPVVFDRAK GDLLYSEDGR AYIDFFAGAG
     ALNYGHNNDY IKDRILDYLT SDRIMHGLDM YTMAKREFIQ SFSERILEPK KLNYKLQFCG
     PTGTNAVEAA LKLARKAKKR TGVFAFMGGF HGMSLGSLSA TSSKSMREGA GLPLGGITFM
     PHPSGAFAGM DTLGYIENIL NDSHSGIDKP AAILLETVQA EGGIHVVDAQ WLRGLHQLCR
     RHDILLITDE IQVGCGRTGG FFSFERAGIE PDLITLSKSI SGYGLPMSLL LLKPELDLWT
     PGEHNGTFRG NQLAFVAAKA ALEFRDRAAL EAQVKQKEEF VRSFLDKEIK PLHPSIEIRG
     LGLIWGIDVS GFTDEAGAKR MTELCFENGL IIERAGRGDR VLKIMPPLTV SMEHLAAGCD
     IIKSSMQQVI SQETQDLLVT T
//
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