ECTB_HALED
ID ECTB_HALED Reviewed; 421 AA.
AC O52250; E1VCW8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Diaminobutyrate--2-oxoglutarate transaminase;
DE EC=2.6.1.76 {ECO:0000269|PubMed:9864317};
DE AltName: Full=DABA aminotransferase;
DE AltName: Full=Diaminobutyrate--2-oxoglutarate aminotransferase;
DE AltName: Full=L-2,4-diaminobutyric acid transaminase;
GN Name=ectB; OrderedLocusNames=HELO_2589;
OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS / 1H9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=768066;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=9570121; DOI=10.1111/j.1574-6968.1998.tb12960.x;
RA Goeller K., Ofer A., Galinski E.A.;
RT "Construction and characterization of an NaCl-sensitive mutant of Halomonas
RT elongata impaired in ectoine biosynthesis.";
RL FEMS Microbiol. Lett. 161:293-300(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA Kunte H.J.;
RT "A blueprint of ectoine metabolism from the genome of the industrial
RT producer Halomonas elongata DSM 2581(T).";
RL Environ. Microbiol. 13:1973-1994(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND CHARACTERIZATION.
RC STRAIN=OUT30018;
RX PubMed=9864317; DOI=10.1128/jb.181.1.91-99.1999;
RA Ono H., Sawada K., Khunajakr N., Tao T., Yamamoto M., Hiramoto M.,
RA Shinmyo A., Takano M., Murooka Y.;
RT "Characterization of biosynthetic enzymes for ectoine as a compatible
RT solute in a moderately halophilic eubacterium, Halomonas elongata.";
RL J. Bacteriol. 181:91-99(1999).
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. Seems to use L-glutamate specifically as the amino
CC group donor to ASA, as it is not active with L-alanine, L-glutamine, L-
CC aspartate and L-lysine, and is only poorly active with L-homoserine. In
CC the reverse reaction, gamma-aminobutyric acid (GABA) and L-ornithine
CC can also be used as amino group donors to 2-oxoglutarate, but with a
CC reduced activity compared to that with DABA.
CC {ECO:0000269|PubMed:9864317}.
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:0000269|PubMed:9864317};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:9864317};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.1 mM for L-glytamate {ECO:0000269|PubMed:9864317};
CC KM=4.5 mM for DL-ASA {ECO:0000269|PubMed:9864317};
CC Vmax=12 umol/min/mg enzyme toward DL-ASA
CC {ECO:0000269|PubMed:9864317};
CC pH dependence:
CC Optimum pH is 8.6-8.7. {ECO:0000269|PubMed:9864317};
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius.
CC {ECO:0000269|PubMed:9864317};
CC -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC ectoine from L-aspartate 4-semialdehyde: step 1/3.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:9864317}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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; AF031489; AAC15882.1; -; Genomic_DNA.
DR EMBL; FN869568; CBV42473.1; -; Genomic_DNA.
DR RefSeq; WP_013332345.1; NC_014532.2.
DR AlphaFoldDB; O52250; -.
DR SMR; O52250; -.
DR STRING; 768066.HELO_2589; -.
DR PRIDE; O52250; -.
DR EnsemblBacteria; CBV42473; CBV42473; HELO_2589.
DR KEGG; hel:HELO_2589; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_6; -.
DR OMA; ELDQWKP; -.
DR BioCyc; MetaCyc:MON-801; -.
DR BRENDA; 2.6.1.76; 2569.
DR UniPathway; UPA00067; UER00121.
DR Proteomes; UP000008707; 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; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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; 1.
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 1: Evidence at protein level;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..421
FT /note="Diaminobutyrate--2-oxoglutarate transaminase"
FT /id="PRO_0000120523"
FT MOD_RES 267
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 421 AA; 46166 MW; A4A2E21596E1E16C CRC64;
MQTQILERME SDVRTYSRSF PVVFTKARNA RLTDEEGREY IDFLAGAGTL NYGHNNPHLK
QALLDYIDSD GIVHGLDFWT AAKRDYLETL EEVILKPRGL DYKVHLPGPT GTNAVEAAIR
LARVAKGRHN IVSFTNGFHG VTMGALATTG NRKFREATGG VPTQAASFMP FDGYLGSSTD
TLDYFEKLLG DKSGGLDVPA AVIVETVQGE GGINVAGLEW LKRLESICRA NDILLIIDDI
QAGCGRTGKF FSFEHAGITP DIVTNSKSLS GYGLPFAHVL MRPELDKWKP GQYNGTFRGF
NLAFATAAAA MRKYWSDDTF ERDVQRKARI VEERFGKIAA WLSENGIEAS ERGRGLMRGI
DVGSGDIADK ITHQAFENGL IIETSGQDGE VVKCLCPLTI PDEDLVEGLD ILETSTKQAF
S
