GLMD_THEKO
ID GLMD_THEKO Reviewed; 326 AA.
AC Q5JDU3;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Glucosamine-6-phosphate deaminase {ECO:0000303|PubMed:16199574};
DE EC=3.5.99.6 {ECO:0000269|PubMed:16199574};
DE AltName: Full=GlcN6P deaminase {ECO:0000303|PubMed:16199574};
GN Name=glmD {ECO:0000303|PubMed:16199574};
GN OrderedLocusNames=TK1755 {ECO:0000312|EMBL:BAD85944.1};
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP SUBUNIT, AND INDUCTION.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=16199574; DOI=10.1128/jb.187.20.7038-7044.2005;
RA Tanaka T., Takahashi F., Fukui T., Fujiwara S., Atomi H., Imanaka T.;
RT "Characterization of a novel glucosamine-6-phosphate deaminase from a
RT hyperthermophilic archaeon.";
RL J. Bacteriol. 187:7038-7044(2005).
CC -!- FUNCTION: Catalyzes the reversible isomerization-deamination of
CC glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P)
CC and ammonium ion. Involved in chitin degradation.
CC {ECO:0000269|PubMed:16199574}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-
CC phosphate + NH4(+); Xref=Rhea:RHEA:12172, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57634, ChEBI:CHEBI:75989; EC=3.5.99.6;
CC Evidence={ECO:0000269|PubMed:16199574};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.339 mM for GlcN6P {ECO:0000269|PubMed:16199574};
CC KM=1.10 mM for Fru6P (in the presence of 170 mM ammonia)
CC {ECO:0000269|PubMed:16199574};
CC KM=17.0 mM for ammonia (in the presence of 8 mM Fru6P)
CC {ECO:0000269|PubMed:16199574};
CC Note=kcat is 97.5 sec(-1) with GlcN6P as substrate. kcat is 44.2
CC sec(-1) with Fru6P as substrate. kcat is 39.6 sec(-1) with ammonia as
CC substrate. {ECO:0000269|PubMed:16199574};
CC pH dependence:
CC Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:16199574};
CC Temperature dependence:
CC Optimum temperature is 95-100 degrees Celsius.
CC {ECO:0000269|PubMed:16199574};
CC -!- PATHWAY: Glycan degradation; chitin degradation.
CC {ECO:0000269|PubMed:16199574}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16199574}.
CC -!- INDUCTION: Expression is induced by diacetylchitobiose (GlcNAc2) but
CC not by chitobiose or maltose. {ECO:0000269|PubMed:16199574}.
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DR EMBL; AP006878; BAD85944.1; -; Genomic_DNA.
DR RefSeq; WP_011250706.1; NC_006624.1.
DR AlphaFoldDB; Q5JDU3; -.
DR SMR; Q5JDU3; -.
DR STRING; 69014.TK1755; -.
DR EnsemblBacteria; BAD85944; BAD85944; TK1755.
DR GeneID; 3235174; -.
DR KEGG; tko:TK1755; -.
DR PATRIC; fig|69014.16.peg.1711; -.
DR eggNOG; arCOG00058; Archaea.
DR HOGENOM; CLU_012520_2_3_2; -.
DR InParanoid; Q5JDU3; -.
DR OMA; WTVGLAH; -.
DR OrthoDB; 42859at2157; -.
DR PhylomeDB; Q5JDU3; -.
DR BioCyc; MetaCyc:MON-16782; -.
DR SABIO-RK; Q5JDU3; -.
DR UniPathway; UPA00349; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF53697; SSF53697; 1.
DR PROSITE; PS51464; SIS; 2.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Hydrolase; Reference proteome; Repeat.
FT CHAIN 1..326
FT /note="Glucosamine-6-phosphate deaminase"
FT /id="PRO_0000448975"
FT DOMAIN 27..169
FT /note="SIS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 180..317
FT /note="SIS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
SQ SEQUENCE 326 AA; 36751 MW; AB8F5FE6F0C770C9 CRC64;
MHATLREIKR TPEGIKTAQR AFEEFVTNSD FLLPREVVYT GCGSSHFLSQ PLAMATTRLG
GRGVALPCSE LLYSREYYPV GKPELLVSIS RSGETTEAVK ALESLDVPKF ALTAYESTLS
RKADYALIVP THEESVVMTH SFTAFYFAFL QLLNASFGLE TYDAEMTSEL TREALKNEGY
IREITGEFDF RNVIFLGSGI LYPIALEAML KMKEMALFWS EAYQTFEVRH GFKSVADEGT
LVVLLVNEPF DWHEKLTKEF QGQGARVLTI GNGDTGADYF IDLPKVDELL TPILHLPIIQ
LLSYYKAIKR GLNPDQPRFL SKVVKW
