GLCAE_SULAC
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 25-MAY-2022, entry version 73.
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; Crenarchaeota; 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}.
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DR EMBL; CP000077; AAY79572.1; -; Genomic_DNA.
DR RefSeq; WP_011277073.1; NC_007181.1.
DR AlphaFoldDB; Q4JCA7; -.
DR SMR; Q4JCA7; -.
DR STRING; 330779.Saci_0151; -.
DR EnsemblBacteria; AAY79572; AAY79572; Saci_0151.
DR GeneID; 3474403; -.
DR KEGG; sai:Saci_0151; -.
DR PATRIC; fig|330779.12.peg.143; -.
DR eggNOG; arCOG00052; Archaea.
DR HOGENOM; CLU_059687_0_0_2; -.
DR OMA; FPELNHN; -.
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 Pfam; PF10432; bact-PGI_C; 1.
DR Pfam; PF01380; SIS; 1.
DR SUPFAM; SSF53697; SSF53697; 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
