ID   GLCAE_SULTO             Reviewed;         311 AA.
AC   Q96YC2; F9VPC2;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=D-glucosamine-6-phosphate 4-epimerase {ECO:0000305};
DE            EC=5.1.3.42 {ECO:0000269|PubMed:29507091};
GN   OrderedLocusNames=STK_22450; ORFNames=ST2245 {ECO:0000303|PubMed:29507091};
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE OF 1-10, FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=29507091; DOI=10.1128/jb.00048-18;
RA   Dadashipour M., Iwamoto M., Hossain M.M., Akutsu J.I., Zhang Z.,
RA   Kawarabayasi Y.;
RT   "Identification of a direct biosynthetic pathway for UDP-N-
RT   acetylgalactosamine from glucosamine-6-phosphate in thermophilic
RT   crenarchaeon Sulfolobus tokodaii.";
RL   J. Bacteriol. 200:E00048-E00048(2018).
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). {ECO:0000269|PubMed:29507091}.
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:0000269|PubMed:29507091};
CC   -!- SIMILARITY: Belongs to the PGI/PMI family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000023; BAK54769.1; -; Genomic_DNA.
DR   RefSeq; WP_010980330.1; NC_003106.2.
DR   AlphaFoldDB; Q96YC2; -.
DR   SMR; Q96YC2; -.
DR   STRING; 273063.STK_22450; -.
DR   EnsemblBacteria; BAK54769; BAK54769; STK_22450.
DR   GeneID; 1460327; -.
DR   KEGG; sto:STK_22450; -.
DR   PATRIC; fig|273063.9.peg.2546; -.
DR   eggNOG; arCOG00052; Archaea.
DR   OMA; FPELNHN; -.
DR   OrthoDB; 55807at2157; -.
DR   BioCyc; MetaCyc:MON-20590; -.
DR   BRENDA; 5.1.3.42; 15396.
DR   Proteomes; UP000001015; 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; cd05017; SIS_PGI_PMI_1; 1.
DR   CDD; cd05637; SIS_PGI_PMI_2; 1.
DR   InterPro; IPR019490; Glu6P/Mann6P_isomerase_C.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   InterPro; IPR035484; SIS_PGI/PMI_1.
DR   Pfam; PF10432; bact-PGI_C; 1.
DR   SUPFAM; SSF53697; SSF53697; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Isomerase; Reference proteome.
FT   CHAIN           1..311
FT                   /note="D-glucosamine-6-phosphate 4-epimerase"
FT                   /id="PRO_0000227797"
FT   DOMAIN          19..141
FT                   /note="SIS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   ACT_SITE        198
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        214
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        294
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   311 AA;  35140 MW;  7539CA4B9C7C6328 CRC64;
     MNNPYENWIN FFQEALNTNI PSIEKIEELV YLGIGGSGIP GRILEILELP VKYQLFRGYK
     VKVNEKSTVI AVSYSGNTTE TIFALLTSLK KTRKAIVITS GGKIEEIASK HNLPVIKLPK
     GLQTRFVFPY IFTYLIRIIN EGLGTNYNVN ELVEGIKDYS KLNEISGILA SQIIGKIPII
     YSSTFLPIAE RFKQEINENA KYPAFYNELP EANHNEIELY SYPSPYTFYP IVIVSDKLDE
     ESANLINAYK IYPLYQSILK NIASLTLLAG LTSVKLAMLL GVKPEQLNII PKIREKTFKL
     FEGDINADQN L