DAPX_BACSU
ID DAPX_BACSU Reviewed; 393 AA.
AC P16524;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Probable N-acetyl-LL-diaminopimelate aminotransferase {ECO:0000305};
DE EC=2.6.1.- {ECO:0000305|PubMed:29280348};
DE AltName: Full=Putative aminotransferase A;
GN Name=dapX {ECO:0000303|PubMed:29280348}; Synonyms=patA, uat;
GN OrderedLocusNames=BSU14000;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Scanlan E., Devine K.M.;
RT "Sequence of the Bacillus subtilis chromosome from ykuA to cse-15.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 99 AND 280.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-393.
RX PubMed=2104615; DOI=10.1128/jb.172.1.86-93.1990;
RA Antoniewski C., Savelli B., Stragier P.;
RT "The spoIIJ gene, which regulates early developmental steps in Bacillus
RT subtilis, belongs to a class of environmentally responsive genes.";
RL J. Bacteriol. 172:86-93(1990).
RN [5]
RP PUTATIVE FUNCTION.
RX PubMed=14627808; DOI=10.1093/nar/gkg900;
RA Rodionov D.A., Vitreschak A.G., Mironov A.A., Gelfand M.S.;
RT "Regulation of lysine biosynthesis and transport genes in bacteria: yet
RT another RNA riboswitch?";
RL Nucleic Acids Res. 31:6748-6757(2003).
RN [6]
RP FUNCTION IN LYSINE BIOSYNTHESIS.
RA Danchin A.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=29280348; DOI=10.1111/1751-7915.13043;
RA Borriss R., Danchin A., Harwood C.R., Medigue C., Rocha E.P.C.,
RA Sekowska A., Vallenet D.;
RT "Bacillus subtilis, the model Gram-positive bacterium: 20 years of
RT annotation refinement.";
RL Microb. Biotechnol. 11:3-17(2018).
CC -!- FUNCTION: Essential for murein biosynthesis (PubMed:29280348). Probably
CC catalyzes the conversion of L-2-acetamido-6-oxopimelate to N-acetyl-LL-
CC 2,6-diaminopimelate (Probable). {ECO:0000269|PubMed:29280348,
CC ECO:0000305|PubMed:29280348, ECO:0000305|Ref.6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N-acetyl-(2S,6S)-2,6-diaminoheptanedioate =
CC L-2-acetamido-6-oxoheptanedioate + L-glutamate; Xref=Rhea:RHEA:25315,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58117,
CC ChEBI:CHEBI:58767; Evidence={ECO:0000305|PubMed:29280348};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:H3ZPU1};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC (acetylase route): step 2/3. {ECO:0000305|PubMed:29280348}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:H3ZPU1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AJ222587; CAA10863.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13273.2; -; Genomic_DNA.
DR EMBL; M29450; AAA22801.1; -; Genomic_DNA.
DR PIR; C69672; C69672.
DR RefSeq; NP_389283.2; NC_000964.3.
DR RefSeq; WP_003232415.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P16524; -.
DR SMR; P16524; -.
DR STRING; 224308.BSU14000; -.
DR PaxDb; P16524; -.
DR PRIDE; P16524; -.
DR EnsemblBacteria; CAB13273; CAB13273; BSU_14000.
DR GeneID; 939235; -.
DR KEGG; bsu:BSU14000; -.
DR PATRIC; fig|224308.179.peg.1526; -.
DR eggNOG; COG0436; Bacteria.
DR InParanoid; P16524; -.
DR OMA; SQGANQY; -.
DR PhylomeDB; P16524; -.
DR BioCyc; BSUB:BSU14000-MON; -.
DR UniPathway; UPA00034; UER00023.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aminotransferase; Cytoplasm;
KW Diaminopimelate biosynthesis; Lysine biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..393
FT /note="Probable N-acetyl-LL-diaminopimelate
FT aminotransferase"
FT /id="PRO_0000123922"
FT MOD_RES 231
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 99
FT /note="Missing (in Ref. 1; CAA10863)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="F -> L (in Ref. 1; CAA10863)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 43536 MW; AD10B69D59B4AA77 CRC64;
MEHLLNPKAR EIEISGIRKF SNLVAQHEDV ISLTIGQPDF FTPHHVKAAA KKAIDENVTS
YTPNAGYLEL RQAVQLYMKK KADFNYDAES EIIITTGASQ AIDAAFRTIL SPGDEVIMPG
PIYPGYEPII NLCGAKPVIV DTTSHGFKLT ARLIEDALTP NTKCVVLPYP SNPTGVTLSE
EELKSIAALL KGRNVFVLSD EIYSELTYDR PHYSIATYLR DQTIVINGLS KSHSMTGWRI
GFLFAPKDIA KHILKVHQYN VSCASSISQK AALEAVTNGF DDALIMREQY KKRLDYVYDR
LVSMGLDVVK PSGAFYIFPS IKSFGMTSFD FSMALLEDAG VALVPGSSFS TYGEGYVRLS
FACSMDTLRE GLDRLELFVL KKREAMQTIN NGV
