ID L9WBJ4_9EURY Unreviewed; 454 AA.
AC L9WBJ4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:ELY45678.1};
GN ORFNames=C495_07855 {ECO:0000313|EMBL:ELY45678.1};
OS Natronorubrum sulfidifaciens JCM 14089.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronorubrum.
OX NCBI_TaxID=1230460 {ECO:0000313|EMBL:ELY45678.1, ECO:0000313|Proteomes:UP000011661};
RN [1] {ECO:0000313|EMBL:ELY45678.1, ECO:0000313|Proteomes:UP000011661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14089 {ECO:0000313|EMBL:ELY45678.1,
RC ECO:0000313|Proteomes:UP000011661};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELY45678.1}.
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DR EMBL; AOHX01000033; ELY45678.1; -; Genomic_DNA.
DR RefSeq; WP_008161664.1; NZ_AOHX01000033.1.
DR AlphaFoldDB; L9WBJ4; -.
DR STRING; 1230460.C495_07855; -.
DR PATRIC; fig|1230460.4.peg.1585; -.
DR eggNOG; arCOG00767; Archaea.
DR OrthoDB; 10363at2157; -.
DR Proteomes; UP000011661; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03087; PGM_like1; 1.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR024086; GlmM_arc-type.
DR NCBIfam; TIGR03990; Arch_GlmM; 1.
DR PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000011661}.
FT DOMAIN 2..128
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 150..250
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 254..360
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 389..447
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 454 AA; 48034 MW; A3B23092B412A4DE CRC64;
MQVFGSSGTR GVANEELTPA FVLRVAKAAG TAWEADRVAI ARDTRYTGRM LADAAASGLA
STGTDVDRLG IIPTPGAQAY ADREGVPVMM ITASHNPPQY NGVKLVGSDG IELVVSDLEE
IEQVLLAEGF AVAPWDETGR SRAVDGVRAT YIDELLAAAD REPIADADLT VALDPGHGAG
ALTSPEFFRK LGCRVVTVNG QADGKFPGRN PEPVPDNLEE LGTLVRATDA DVGIAHDGDA
DRAIFFDETG AYVNGDATLA ALAAAELEAG DTTVSAVNVS QRLVDVVTEV GAELELTPIG
STNIITRIEE LEAKGEHVPI AGEGNGGIFF PSFRLTRDGA FTAARFLELV AERPVSEIVA
PYDGYANVRH NLAYESTAER DAMLDAAANH AQSSDADLNT RDGYRLDHGD AWVLARPSGT
EPLVRVYAEA RDTERARELA NELYETLSDA KADA
//