GLCAE_SACS2
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 03-AUG-2022, entry version 88.
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; Crenarchaeota; 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}.
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; AE006641; AAK42443.1; -; Genomic_DNA.
DR PIR; D90398; D90398.
DR RefSeq; WP_009991835.1; NC_002754.1.
DR AlphaFoldDB; Q97WE5; -.
DR SMR; Q97WE5; -.
DR STRING; 273057.SSO2281; -.
DR EnsemblBacteria; AAK42443; AAK42443; SSO2281.
DR GeneID; 44128013; -.
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 OMA; FPELNHN; -.
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 InterPro; IPR019490; Glu6P/Mann6P_isomerase_C.
DR InterPro; IPR046348; SIS_dom_sf.
DR Pfam; PF10432; bact-PGI_C; 1.
DR SUPFAM; SSF53697; SSF53697; 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"
FT ACT_SITE 208
FT /note="Proton donor"
FT /evidence="ECO:0000250"
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