ECTB_CHRSD
ID ECTB_CHRSD Reviewed; 423 AA.
AC Q9ZEU7; Q1QWC9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Diaminobutyrate--2-oxoglutarate transaminase;
DE EC=2.6.1.76;
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=Csal_1877;
OS Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS NCIMB 13768 / 1H11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=290398;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9924816; DOI=10.1016/s0723-2020(98)80060-x;
RA Canovas D., Vargas C., Calderon M.I., Ventosa A., Nieto J.J.;
RT "Characterization of the genes for the biosynthesis of the compatible
RT solute ectoine in the moderately halophilic bacterium Halomonas elongata
RT DSM 3043.";
RL Syst. Appl. Microbiol. 21:487-497(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX PubMed=22675587; DOI=10.4056/sigs.2285059;
RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT "Complete genome sequence of the halophilic and highly halotolerant
RT Chromohalobacter salexigens type strain (1H11(T)).";
RL Stand. Genomic Sci. 5:379-388(2011).
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:0000250}.
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;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC ectoine from L-aspartate 4-semialdehyde: step 1/3.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AJ011103; CAA09484.1; -; Genomic_DNA.
DR EMBL; CP000285; ABE59229.1; -; Genomic_DNA.
DR RefSeq; WP_011507175.1; NC_007963.1.
DR PDB; 6RL5; X-ray; 2.45 A; A/B/C/D/E/F/G/H=1-423.
DR PDBsum; 6RL5; -.
DR AlphaFoldDB; Q9ZEU7; -.
DR SMR; Q9ZEU7; -.
DR STRING; 290398.Csal_1877; -.
DR EnsemblBacteria; ABE59229; ABE59229; Csal_1877.
DR KEGG; csa:Csal_1877; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_6; -.
DR OMA; ELDQWKP; -.
DR OrthoDB; 386839at2; -.
DR UniPathway; UPA00067; UER00121.
DR Proteomes; UP000000239; 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 3D-structure; Aminotransferase; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..423
FT /note="Diaminobutyrate--2-oxoglutarate transaminase"
FT /id="PRO_0000120522"
FT MOD_RES 267
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:6RL5"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:6RL5"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:6RL5"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:6RL5"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6RL5"
FT HELIX 111..126
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:6RL5"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:6RL5"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:6RL5"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:6RL5"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:6RL5"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:6RL5"
FT HELIX 218..229
FT /evidence="ECO:0007829|PDB:6RL5"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:6RL5"
FT TURN 240..247
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:6RL5"
FT HELIX 252..256
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:6RL5"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:6RL5"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:6RL5"
FT TURN 296..299
FT /evidence="ECO:0007829|PDB:6RL5"
FT HELIX 301..314
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:6RL5"
FT HELIX 319..344
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 350..354
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:6RL5"
FT HELIX 365..377
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 383..389
FT /evidence="ECO:0007829|PDB:6RL5"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:6RL5"
FT HELIX 402..419
FT /evidence="ECO:0007829|PDB:6RL5"
SQ SEQUENCE 423 AA; 46200 MW; 735C6BCF5A88288C CRC64;
MQTQILERME SEVRTYSRSF PTVFTEAKGA RLHAEDGNQY IDFLAGAGTL NYGHNHPKLK
QALADYIASD GIVHGLDMWS AAKRDYLETL EEVILKPRGL DYKVHLPGPT GTNAVEAAIR
LARNAKGRHN IVTFTNGFHG VTMGALATTG NRKFREATGG IPTQGASFMP FDGYMGEGVD
TLSYFEKLLG DNSGGLDVPA AVIIETVQGE GGINPAGIPW LQRLEKICRD HDMLLIVDDI
QAGCGRTGKF FSFEHAGITP DIVTNSKSLS GFGLPFAHVL MRPELDIWKP GQYNGTFRGF
NLAFVTAAAA MRHFWSDDTF ERDVQRKGRV VEDRFQKLAS FMTEKGHPAS ERGRGLMRGL
DVGDGDMADK ITAQAFKNGL IIETSGHSGQ VIKCLCPLTI TDEDLVGGLD ILEQSVKEVF
GQA
