ID   GLCAE_SULAC             Reviewed;         306 AA.
AC   Q4JCA7;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=Saci_0151;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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}.
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; CP000077; AAY79572.1; -; Genomic_DNA.
DR   RefSeq; WP_011277073.1; NZ_CP046615.1.
DR   AlphaFoldDB; Q4JCA7; -.
DR   SMR; Q4JCA7; -.
DR   STRING; 330779.Saci_0151; -.
DR   GeneID; 78440503; -.
DR   KEGG; sai:Saci_0151; -.
DR   PATRIC; fig|330779.12.peg.143; -.
DR   eggNOG; arCOG00052; Archaea.
DR   HOGENOM; CLU_059687_0_0_2; -.
DR   Proteomes; UP000001018; 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   NCBIfam; TIGR02128; G6PI_arch; 1.
DR   Pfam; PF10432; bact-PGI_C; 1.
DR   Pfam; PF01380; SIS; 1.
DR   SUPFAM; SSF53697; SIS domain; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome.
FT   CHAIN           1..306
FT                   /note="D-glucosamine-6-phosphate 4-epimerase"
FT                   /id="PRO_0000227795"
FT   DOMAIN          19..153
FT                   /note="SIS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   ACT_SITE        200
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        216
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        296
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   306 AA;  34158 MW;  771F0D94933A67A4 CRC64;
     MSNVYERWKE FYEDAISRDI PGVKTAEKIA YFGIGGSGIP GEVLKLLDLP VEYKLFRSYK
     VNVDSKTTVV AVSYSGNTAE TLAGVKRAQE LGVKEIIVIT SGGKLKEIAE SKGYPLLSLP
     QGYQTRFIFP YIFTYLVRIL NQSTGSNYRV QDLVDGIQDN FTMLSEVSTR IANRITGKVP
     IFYASDLLPI AERFKQEVNE NAKYPAFFSQ LPEANHNEIE LYSSQQGNQF IPIVIPSDKI
     DEATASLINA ELIYPPYKSI LKNISGMFLI AGLASVKLAS QLNIKAEELR IIPKIRERTH
     NLLMGG
//