ID   GLCAE_SACS2             Reviewed;         296 AA.
AC   Q97WE5;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   28-JAN-2026, entry version 99.
DE   RecName: Full=D-glucosamine-6-phosphate 4-epimerase {ECO:0000250|UniProtKB:Q96YC2};
DE            EC=5.1.3.42 {ECO:0000250|UniProtKB:Q96YC2};
GN   OrderedLocusNames=SSO2281;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
CC   -!- FUNCTION: Involved in the synthesis of UDP-N-acetylgalactosamine (UDP-
CC       GalNAc). Catalyzes the conversion of glucosamine-6-phosphate (GlcN-6-P)
CC       to galactosamine-6-phosphate (GalN-6-P).
CC       {ECO:0000250|UniProtKB:Q96YC2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucosamine 6-phosphate = D-galactosamine 6-phosphate;
CC         Xref=Rhea:RHEA:18789, ChEBI:CHEBI:58725, ChEBI:CHEBI:71674;
CC         EC=5.1.3.42; Evidence={ECO:0000250|UniProtKB:Q96YC2};
CC   -!- SIMILARITY: Belongs to the PGI/PMI family. {ECO:0000305}.
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DR   EMBL; AE006641; AAK42443.1; -; Genomic_DNA.
DR   PIR; D90398; D90398.
DR   RefSeq; WP_009991835.1; NC_002754.1.
DR   AlphaFoldDB; Q97WE5; -.
DR   SMR; Q97WE5; -.
DR   FunCoup; Q97WE5; 163.
DR   STRING; 273057.SSO2281; -.
DR   PaxDb; 273057-SSO2281; -.
DR   EnsemblBacteria; AAK42443; AAK42443; SSO2281.
DR   GeneID; 1453770; -.
DR   KEGG; sso:SSO2281; -.
DR   PATRIC; fig|273057.12.peg.2374; -.
DR   eggNOG; arCOG00052; Archaea.
DR   HOGENOM; CLU_059687_0_0_2; -.
DR   InParanoid; Q97WE5; -.
DR   PhylomeDB; Q97WE5; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:InterPro.
DR   GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IEA:InterPro.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05637; SIS_PGI_PMI_2; 1.
DR   Gene3D; 3.40.50.10490; Glucose-6-phosphate isomerase like protein, domain 1; 2.
DR   InterPro; IPR019490; Glu6P/Mann6P_isomerase_C.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   NCBIfam; TIGR02128; G6PI_arch; 1.
DR   NCBIfam; NF006422; PRK08674.1-1; 1.
DR   Pfam; PF10432; bact-PGI_C; 1.
DR   SUPFAM; SSF53697; SIS domain; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome.
FT   CHAIN           1..296
FT                   /note="D-glucosamine-6-phosphate 4-epimerase"
FT                   /id="PRO_0000227796"
FT   DOMAIN          12..143
FT                   /note="SIS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   ACT_SITE        192
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZWV0"
FT   ACT_SITE        208
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZWV0"
FT   ACT_SITE        286
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   296 AA;  33141 MW;  E4EA89F3BA2F215B CRC64;
     MDEIYLNWDK MFDEAFRIPI HEIKNDNIVF SGIGGSGIVG EIANILGVEL SFKRKFTGKE
     SLIAVSYSGT TSETINDVEN AVKAGSEVII ITSGGILEKL AKEKSLKLIK IPSGFQTRYA
     FPYLFTPLIK MTTKRRGIKI NEMELKEGVI EAKEQIKADA TRLAELLINR IPVIYSSKYL
     AIAKRFKQEI NENAKHPAFY GEIPEINHNE IESYVHGPSL VSVIVESSEI DKITEDVLNS
     IVIKPYFNSD EKNISSLLAL AGVTSLEMAK KLNEKPDKLY NIPKARQLTS NLFKIN
//