ID   DAT_HAEIN               Reviewed;         454 AA.
AC   P44951;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Diaminobutyrate--2-oxoglutarate aminotransferase;
DE            EC=2.6.1.76;
DE   AltName: Full=Diaminobutyrate transaminase;
DE   AltName: Full=L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase;
DE            Short=DABA aminotransferase;
DE            Short=DABA-AT;
DE   AltName: Full=L-diaminobutyric acid transaminase;
GN   Name=dat; OrderedLocusNames=HI_0949;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=9514614; DOI=10.1248/bpb.21.170;
RA   Ikai H., Yamamoto S.;
RT   "Two genes involved in the 1,3-diaminopropane production pathway in
RT   Haemophilus influenzae.";
RL   Biol. Pharm. Bull. 21:170-173(1998).
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:0000305};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; 1,3-diaminopropane
CC       biosynthesis; 1,3-diaminopropane from L-aspartate 4-semialdehyde: step
CC       1/2.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; L42023; AAC22610.1; -; Genomic_DNA.
DR   PIR; C64104; C64104.
DR   RefSeq; NP_439110.1; NC_000907.1.
DR   RefSeq; WP_005693298.1; NC_000907.1.
DR   AlphaFoldDB; P44951; -.
DR   SMR; P44951; -.
DR   STRING; 71421.HI_0949; -.
DR   EnsemblBacteria; AAC22610; AAC22610; HI_0949.
DR   KEGG; hin:HI_0949; -.
DR   PATRIC; fig|71421.8.peg.991; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_6; -.
DR   OMA; NLMPGVQ; -.
DR   PhylomeDB; P44951; -.
DR   BioCyc; HINF71421:G1GJ1-990-MON; -.
DR   UniPathway; UPA00010; UER00731.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0045303; F:diaminobutyrate-2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43552; PTHR43552; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00709; dat; 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..454
FT                   /note="Diaminobutyrate--2-oxoglutarate aminotransferase"
FT                   /id="PRO_0000120515"
FT   MOD_RES         287
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   454 AA;  49369 MW;  B4B26F3AB7C55063 CRC64;
     MTMITPVQAI LASNQHFLDR QDVMESNVRS YPRKLPFAYA KAQGCWVTDV EGNEYLDFLA
     GAGTLALGHN HPILMQAIKD VLDSGLPLHT LDLTTPLKDA FSEELLSFFP KDKYILQFTG
     PSGADANEAA IKLAKTYTGR GNIIAFSGGF HGMTQGALAL TGNLGAKNAV ENLMPGVQFM
     PYPHEYRCPF GIGGEAGAKA VEQYFENFIE DVESGVVKPA AVILEAIQGE GGVVSAPISF
     LQKVREVTQK HGILMIVDEV QAGFCRSGRM FAFEHAGIEP DIIVMSKAVG GSLPLAVLAI
     RKEFDAWQPA GHTGTFRGNQ LAMATGYASL KIMRDENLAQ NAQERGEYLT NALRELSKEY
     PCIGNVRGRG LMMGIDIVDE RQSKDATGAY PRDCELAAAI QKACFKNKLL LERGGRGGNV
     VRVLCAVNIN QSECEEFIKR FKQSVVDALK VVRS