ID S6CUW9_9EURY Unreviewed; 442 AA.
AC S6CUW9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Phosphomannomutase / phosphoglucosa mine mutase {ECO:0000313|EMBL:CCQ34112.1};
DE EC=5.4.2.- {ECO:0000313|EMBL:CCQ34112.1};
DE EC=5.4.2.10 {ECO:0000313|EMBL:CCQ34112.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:CCQ34112.1};
GN ORFNames=HTIA_1996 {ECO:0000313|EMBL:CCQ34112.1};
OS Halorhabdus tiamatea SARL4B.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorhabdus.
OX NCBI_TaxID=1033806 {ECO:0000313|EMBL:CCQ34112.1, ECO:0000313|Proteomes:UP000015381};
RN [1] {ECO:0000313|EMBL:CCQ34112.1, ECO:0000313|Proteomes:UP000015381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|Proteomes:UP000015381};
RX PubMed=24428220; DOI=10.1111/1462-2920.12393;
RA Werner J., Ferrer M., Michel G., Mann A.J., Huang S., Juarez S.,
RA Ciordia S., Albar J.P., Alcaide M., La Cono V., Yakimov M.M., Antunes A.,
RA Taborda M., Da Costa M.S., Amann R.I., Gloeckner F.O., Golyshina O.V.,
RA Golyshin P.N., Teeling H.;
RT "Halorhabdus tiamatea: proteogenomics and glycosidase activity measurements
RT identify the first cultivated euryarchaeon from a deep-sea anoxic brine
RT lake as potential polysaccharide degrader.";
RL Environ. Microbiol. 16:2525-2537(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, ECO:0000256|RuleBase:RU004326}.
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DR EMBL; HF571520; CCQ34112.1; -; Genomic_DNA.
DR AlphaFoldDB; S6CUW9; -.
DR KEGG; hti:HTIA_1996; -.
DR PATRIC; fig|1033806.12.peg.1982; -.
DR HOGENOM; CLU_016950_7_1_2; -.
DR Proteomes; UP000015381; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
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; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR024086; GlmM_arc-type.
DR NCBIfam; TIGR03990; Arch_GlmM; 1.
DR PANTHER; PTHR42946:SF6; PHOSPHOGLUCOSAMINE MUTASE; 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.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:CCQ34112.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 9..135
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 155..248
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 253..356
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 368..437
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 442 AA; 46435 MW; CE23C1155CAF8AD0 CRC64;
MPGRRGVDMF GTSGIRGPVG ETVTADLALS VGRALGIDAG RVVVGRDPRE SGQFLLDALT
AGLRETGTDV IDLGVAATPT VARAVRGKDG DAGVVITASH NPPADNGIKL WQPTTQAFDT
ARQETIADRI EAGEFDPAAW DELGTRRRQG HTEAHIEAIL DAVEVASPPE VVVDLGNGAG
QVSVDALTRL GSDVETLNAQ PDGAFPGRPS EPTAENCASL TGLARETGRL GIAHDGDADR
LRAVTEDGEF VGGDTLLAIF AREAADPGET VAAPVNTSLA VDDYLAAEDV DVVRTRVGDV
SVAERASEPG VAFGGEPSGA WIWPAEALCP DGPLAAAKLV ELAAERPLAD RVADVETYPI
HRDSVSVTEK AVVMEWVHEA VEDRYDDVTT LDGVRVDLGD AWFLIRASGT QPLVRITAEA
RDPDRATSVF EEAREIVSQA HE
//
