ID F5YYE5_MYCSD Unreviewed; 394 AA.
AC F5YYE5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 Name=argD {ECO:0000313|EMBL:AEF36698.1};
GN OrderedLocusNames=JDM601_2698 {ECO:0000313|EMBL:AEF36698.1};
OS Mycolicibacter sinensis (strain JDM601) (Mycobacterium sinense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacter.
OX NCBI_TaxID=875328 {ECO:0000313|EMBL:AEF36698.1, ECO:0000313|Proteomes:UP000009224};
RN [1] {ECO:0000313|EMBL:AEF36698.1, ECO:0000313|Proteomes:UP000009224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDM601 {ECO:0000313|EMBL:AEF36698.1,
RC ECO:0000313|Proteomes:UP000009224};
RX PubMed=21685274; DOI=10.1128/JB.05291-11;
RA Zhang Z.Y., Sun Z.Q., Wang Z.L., Wen Z.L., Sun Q.W., Zhu Z.Q., Song Y.Z.,
RA Zhao J.W., Wang H.H., Zhang S.L., Guo X.K.;
RT "Complete genome sequence of a novel clinical isolate, the nontuberculous
RT Mycobacterium strain JDM601.";
RL J. Bacteriol. 193:4300-4301(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: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; CP002329; AEF36698.1; -; Genomic_DNA.
DR AlphaFoldDB; F5YYE5; -.
DR STRING; 875328.JDM601_2698; -.
DR KEGG; mjd:JDM601_2698; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_11; -.
DR UniPathway; UPA00067; UER00121.
DR Proteomes; UP000009224; 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; 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:AEF36698.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000009224};
KW Transferase {ECO:0000256|RuleBase:RU365034}.
SQ SEQUENCE 394 AA; 42520 MW; A8A7D2BDC5194237 CRC64;
MWDVDGNEYV DFFAGAGALN YGHNHPDLKA PLVEYLSADR VVHSLDMNTV AKAAFLERFE
EVILKPRGLD YKVQFPGPTG TNAVESALKL ARKVTGKESI ISFTNAFHGM TLGSLSVTGN
SMKRGGAGIP LVHATPMPYD NYLDGVTPDF IWFERLLQDS GSGLNEPAAV IVETVQGEGG
INVARLEWLH GLAELCKRHG LLLIVDDVQM GCGRTGPFFS FEAAGIVPDI VCMSKSISGY
GLPMALTLFK PELDVWEPGE HNGTFRGQNP SFVTATAALN FWTDNLLEKQ VLRKGEQIDQ
ALHEVIEPFD GIETRGRGLI RGVAFERPEL AGAVQKEAFA RGLLLETSGP EGEVVKLMPP
LVIDDEDLAE GLTLAAQSIE AVAAKELTTS GAKA
//
