ID A0A1X7H912_9ACTN Unreviewed; 423 AA.
AC A0A1X7H912;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 ORFNames=SAMN02745830_06438 {ECO:0000313|EMBL:SMF81844.1};
OS Streptomyces sp. Amel2xC10.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1305826 {ECO:0000313|EMBL:SMF81844.1, ECO:0000313|Proteomes:UP000192930};
RN [1] {ECO:0000313|EMBL:SMF81844.1, ECO:0000313|Proteomes:UP000192930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Amel2xC10 {ECO:0000313|EMBL:SMF81844.1,
RC ECO:0000313|Proteomes:UP000192930};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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|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|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|RuleBase:RU365034}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FWZW01000018; SMF81844.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7H912; -.
DR OrthoDB; 9801052at2; -.
DR UniPathway; UPA00067; UER00121.
DR Proteomes; UP000192930; Unassembled WGS sequence.
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; IPR049704; Aminotrans_3_PPA_site.
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:SMF81844.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000192930};
KW Transferase {ECO:0000256|RuleBase:RU365034, ECO:0000313|EMBL:SMF81844.1}.
SQ SEQUENCE 423 AA; 46427 MW; 10EF635F88689803 CRC64;
MTITQPDLSV FETLESEVRS YCRSWPAVFD RAQGSVMHDE DGRRHLDFFA GAGSLNYGHN
NPVLKRALID YLLRDGVTHG LDMSTVAKRT FLSTFQDLVL RPRDLPYKVM FPGPTGTNAV
EAALKLARKV KGREAIVSFT NAFHGMSLGS LAVTGNAFKR AGAGIPLVHG TPMPFDNYFD
GTVPDFLWFE RLLEDQGSGL NKPAAVIVET VQGEGGINVA RPEWLRALKE LCERQDMLLI
VDDIQMGCGR TGAFFSFEES GIVPDIVTVS KSISGYGLPM SLCLFRPELD VWEPGEHNGT
FRGNNPAFVT ATAALEAYWT DGAAMEKQTR ARGEQIEEGL ISITEENLAD VKEYRGRGLV
WGLEFHDKER AGRVAGRAFE LGLLIETSGP ESEVVKLLPA LTITPEELDE GLSVVARAVR
ETA
//
