NAG1_CANAL
ID NAG1_CANAL Reviewed; 248 AA.
AC Q04802; A0A1D8PQG4; Q59RG3; Q59RW3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 3.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Glucosamine-6-phosphate isomerase;
DE EC=3.5.99.6;
DE AltName: Full=Glucosamine-6-phosphate deaminase;
DE Short=GNPDA;
DE Short=GlcN6P deaminase;
GN Name=NAG1; OrderedLocusNames=CAALFM_C604590CA;
GN ORFNames=CaO19.2156, CaO19.9703;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-35.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=7683645; DOI=10.1016/s0021-9258(18)98337-7;
RA Natarajan K., Datta A.;
RT "Molecular cloning and analysis of the NAG1 cDNA coding for glucosamine-6-
RT phosphate deaminase from Candida albicans.";
RL J. Biol. Chem. 268:9206-9214(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RA Jyothi Kumar M., Jamaluddin M.D.S., Natarajan K., Deepinder K., Datta A.;
RT "Discrete inducible factors control the expression of C. albicans NAG1,
RT which lies within a cluster of GlcNAc catabolic genes.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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 -!- SUBUNIT: Monomer.
CC -!- INDUCTION: By N-acetylglucosamine.
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. {ECO:0000305}.
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DR EMBL; L07558; AAA34352.1; -; mRNA.
DR EMBL; AF079804; AAF04334.1; -; Genomic_DNA.
DR EMBL; CP017628; AOW30375.1; -; Genomic_DNA.
DR PIR; A46652; A46652.
DR RefSeq; XP_712431.2; XM_707338.2.
DR AlphaFoldDB; Q04802; -.
DR SMR; Q04802; -.
DR STRING; 237561.Q04802; -.
DR PRIDE; Q04802; -.
DR GeneID; 3645966; -.
DR KEGG; cal:CAALFM_C604590CA; -.
DR CGD; CAL0000199480; NAG1.
DR VEuPathDB; FungiDB:C6_04590C_A; -.
DR eggNOG; KOG3148; Eukaryota.
DR HOGENOM; CLU_049611_0_1_1; -.
DR InParanoid; Q04802; -.
DR OrthoDB; 1425290at2759; -.
DR PHI-base; PHI:221; -.
DR PRO; PR:Q04802; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006043; P:glucosamine catabolic process; IBA:GO_Central.
DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; IBA:GO_Central.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IBA:GO_Central.
DR CDD; cd01399; GlcN6P_deaminase; 1.
DR InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR InterPro; IPR004547; Glucosamine6P_isomerase.
DR InterPro; IPR018321; Glucosamine6P_isomerase_CS.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR11280; PTHR11280; 1.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00502; nagB; 1.
DR PROSITE; PS01161; GLC_GALNAC_ISOMERASE; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Hydrolase;
KW Reference proteome.
FT CHAIN 1..248
FT /note="Glucosamine-6-phosphate isomerase"
FT /id="PRO_0000160121"
FT ACT_SITE 68
FT /note="Proton acceptor; for enolization step"
FT /evidence="ECO:0000250"
FT ACT_SITE 137
FT /note="For ring-opening step"
FT /evidence="ECO:0000250"
FT ACT_SITE 139
FT /note="Proton acceptor; for ring-opening step"
FT /evidence="ECO:0000250"
FT ACT_SITE 144
FT /note="For ring-opening step"
FT /evidence="ECO:0000250"
FT CONFLICT 73
FT /note="L -> F (in Ref. 1; AAA34352 and 2; AAF04334)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 27491 MW; 650B2F6250FB1538 CRC64;
MRQAIFSNPN DAAEYLANYI IAKINSTPRT FVLGLPTGSS PEGIYAKLIE ANKQGRVSFK
NVVTFNMDEY LGLAPSDLQS YHYFMYDKFF NHIDIPRENI HILNGLAANI DEECANYEKK
IKQYGRIDLF LGGLGPEGHL AFNEAGSSRN SKTRKVELVE STIKANCRFF GNDESKVPKY
ALSVGISTIL DNSDEIAIIV LGKNKQFALD KTVNGKPNDP KYPSSYLQDH ANVLIVCDNA
AAGLKSKL
