DGAE_SALT1
ID DGAE_SALT1 Reviewed; 369 AA.
AC D0ZLR3;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=D-glucosaminate-6-phosphate ammonia lyase {ECO:0000303|PubMed:23836865};
DE EC=4.3.1.29 {ECO:0000269|PubMed:23836865};
DE AltName: Full=Glucosaminate-6-phosphate dehydratase {ECO:0000303|PubMed:23836865};
GN Name=dgaE {ECO:0000303|PubMed:23836865}; OrderedLocusNames=STM14_4544;
OS Salmonella typhimurium (strain 14028s / SGSC 2262).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=588858;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14028s / SGSC 2262;
RX PubMed=19897643; DOI=10.1128/jb.01233-09;
RA Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT "Short-term signatures of evolutionary change in the Salmonella enterica
RT serovar typhimurium 14028 genome.";
RL J. Bacteriol. 192:560-567(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=23836865; DOI=10.1128/jb.00290-13;
RA Miller K.A., Phillips R.S., Mrazek J., Hoover T.R.;
RT "Salmonella utilizes D-glucosaminate via a mannose family
RT phosphotransferase system permease and associated enzymes.";
RL J. Bacteriol. 195:4057-4066(2013).
CC -!- FUNCTION: Involved in the catabolism of D-glucosaminate. Catalyzes the
CC conversion of D-glucosaminate 6-phosphate to yield keto-3-
CC deoxygluconate 6-phosphate (KDGP). {ECO:0000269|PubMed:23836865}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-amino-2-deoxy-D-gluconate 6-phosphate = 2-dehydro-3-deoxy-6-
CC phospho-D-gluconate + NH4(+); Xref=Rhea:RHEA:38303,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57569, ChEBI:CHEBI:75705; EC=4.3.1.29;
CC Evidence={ECO:0000269|PubMed:23836865};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P0A821};
CC -!- INDUCTION: By D-glucosaminate and DgaR. {ECO:0000269|PubMed:23836865}.
CC -!- SIMILARITY: Belongs to the SelA family. {ECO:0000305}.
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DR EMBL; CP001363; ACY90925.1; -; Genomic_DNA.
DR RefSeq; WP_000188463.1; NZ_CP043402.1.
DR PDB; 7LCE; X-ray; 2.58 A; A/B/C/D=1-369.
DR PDBsum; 7LCE; -.
DR AlphaFoldDB; D0ZLR3; -.
DR SMR; D0ZLR3; -.
DR EnsemblBacteria; ACY90925; ACY90925; STM14_4544.
DR KEGG; seo:STM14_4544; -.
DR PATRIC; fig|588858.6.peg.4142; -.
DR HOGENOM; CLU_040896_1_0_6; -.
DR OMA; GKKTWIA; -.
DR BioCyc; MetaCyc:MON-18124; -.
DR BioCyc; SENT588858:STM14_RS19905-MON; -.
DR BRENDA; 4.3.1.29; 5542.
DR Proteomes; UP000002695; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR006337; DgaE-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR018319; SelA-like.
DR Pfam; PF03841; SelA; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01437; selA_rel; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Pyridoxal phosphate.
FT CHAIN 1..369
FT /note="D-glucosaminate-6-phosphate ammonia lyase"
FT /id="PRO_0000430794"
FT MOD_RES 213
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0A821"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:7LCE"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 47..62
FT /evidence="ECO:0007829|PDB:7LCE"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:7LCE"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:7LCE"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:7LCE"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:7LCE"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:7LCE"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:7LCE"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:7LCE"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 227..234
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 248..262
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 270..282
FT /evidence="ECO:0007829|PDB:7LCE"
FT STRAND 286..292
FT /evidence="ECO:0007829|PDB:7LCE"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 308..311
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 315..324
FT /evidence="ECO:0007829|PDB:7LCE"
FT STRAND 325..332
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:7LCE"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:7LCE"
FT HELIX 352..365
FT /evidence="ECO:0007829|PDB:7LCE"
SQ SEQUENCE 369 AA; 39323 MW; 751E649271BB3A5D CRC64;
MTPNIYQQLG LKKVINACGK MTILGVSSVA PEVMQATARA ASAFVEIDAL VEKTGELVSR
YTGAEDSYIT SCASAGIAIA VAAAITHGDR ARVALMPDSS GMANEVVMLR GHNVDYGAPV
TSAIRLGGGR IVEVGSSNLA TRWQLESAIN EKTAALLYVK SHHCVQKGML SIDDFVQVAQ
ANHLPLIVDA AAEEDLRGWV ASGADMVIYS GAKAFNAPTS GFITGRKTWI AACKAQHQGI
ARAMKIGKEN MVGLVYALEN YHQGQTTVTA AQLQPVAEAI SAIHGLYADI EQDEAGRAIW
RIRVRVNASE LGLNAQDVEA QLRGGEIAIY ARKYQLHQGV FSLDPRTVAE GEMALIVARL
REIAEHAAD
