DAAA_STAAN
ID DAAA_STAAN Reviewed; 282 AA.
AC P99090; Q99TB4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=D-alanine aminotransferase;
DE EC=2.6.1.21;
DE AltName: Full=D-amino acid aminotransferase;
DE AltName: Full=D-amino acid transaminase;
DE Short=DAAT;
DE AltName: Full=D-aspartate aminotransferase;
GN Name=dat; OrderedLocusNames=SA1571;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=N315;
RX PubMed=15590099; DOI=10.1016/j.mimet.2004.09.017;
RA Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y.,
RA Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C.,
RA Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.;
RT "Correlation of proteomic and transcriptomic profiles of Staphylococcus
RT aureus during the post-exponential phase of growth.";
RL J. Microbiol. Methods 60:247-257(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
CC -!- FUNCTION: Acts on the D-isomers of alanine, leucine, aspartate,
CC glutamate, aminobutyrate, norvaline and asparagine. The enzyme
CC transfers an amino group from a substrate D-amino acid to the pyridoxal
CC phosphate cofactor to form pyridoxamine and an alpha-keto acid in the
CC first half-reaction. The second half-reaction is the reverse of the
CC first, transferring the amino group from the pyridoxamine to a second
CC alpha-keto acid to form the product D-amino acid via a ping-pong
CC mechanism. This is an important process in the formation of D-alanine
CC and D-glutamate, which are essential bacterial cell wall components (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + D-alanine = D-glutamate + pyruvate;
CC Xref=Rhea:RHEA:15869, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29986, ChEBI:CHEBI:57416; EC=2.6.1.21;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; BA000018; BAB42839.1; -; Genomic_DNA.
DR PIR; B89960; B89960.
DR RefSeq; WP_000411084.1; NC_002745.2.
DR AlphaFoldDB; P99090; -.
DR SMR; P99090; -.
DR SWISS-2DPAGE; P99090; -.
DR EnsemblBacteria; BAB42839; BAB42839; BAB42839.
DR KEGG; sau:SA1571; -.
DR HOGENOM; CLU_020844_4_1_9; -.
DR OMA; SMGKMMA; -.
DR Proteomes; UP000000751; Chromosome.
DR GO; GO:0047810; F:D-alanine:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR GO; GO:0046437; P:D-amino acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019478; P:D-amino acid catabolic process; ISS:UniProtKB.
DR Gene3D; 3.20.10.10; -; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR018300; Aminotrans_IV_CS.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR InterPro; IPR005784; D_amino_transT.
DR Pfam; PF01063; Aminotran_4; 1.
DR SUPFAM; SSF56752; SSF56752; 1.
DR TIGRFAMs; TIGR01121; D_amino_aminoT; 1.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Pyridoxal phosphate; Transferase.
FT CHAIN 1..282
FT /note="D-alanine aminotransferase"
FT /id="PRO_0000103255"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT BINDING 51
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT BINDING 178
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT MOD_RES 146
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P19938"
SQ SEQUENCE 282 AA; 31908 MW; 6B0D215F38699A0F CRC64;
MEKIFLNGEF VSPSEAKVSY NDRGYVFGDG IYEYIRVYNG KLFTVTEHYE RFLRSANEIG
LDLNYSVEEL IELSRKLVDM NQIETGAIYI QATRGVAERN HSFPTPEVEP AIVAYTKSYD
RPYDHLENGV NGVTVEDIRW LRCDIKSLNL LGNVLAKEYA VKYNAVEAIQ HRGETVTEGS
SSNAYAIKDG VIYTHPINNY ILNGITRIVI KKIAEDYNIP FKEETFTVDF LKNADEVIVS
STSAEVTPVI KLDGEPINDG KVGPITRQLQ EGFEKYIESH SI
