ID Q9UZB8_PYRAB Unreviewed; 456 AA. AC Q9UZB8; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 120. DE SubName: Full=PMM phosphomannomutase {ECO:0000313|EMBL:CAB50141.1}; DE SubName: Full=Phosphomannomutase (Pmm) {ECO:0000313|EMBL:CCE70671.1}; GN Name=pmm {ECO:0000313|EMBL:CAB50141.1}; GN ORFNames=PAB0819 {ECO:0000313|EMBL:CAB50141.1}; OS Pyrococcus abyssi (strain GE5 / Orsay). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=272844 {ECO:0000313|EMBL:CAB50141.1, ECO:0000313|Proteomes:UP000000810}; RN [1] {ECO:0000313|EMBL:CAB50141.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Orsay {ECO:0000313|EMBL:CAB50141.1}; RA Genoscope; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CAB50141.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Orsay {ECO:0000313|EMBL:CAB50141.1}; RX PubMed=10736225; DOI=10.1006/jmbi.2000.3593; RA Gaspin C., Cavaille J., Erauso G.; RT "Archaeal homologs of eukaryotic methylation guide small nucleolar RNAs: RT lessons from the Pyrococcus genomes."; RL J. Mol. Biol. 297:895-906(2000). RN [3] {ECO:0000313|EMBL:CAB50141.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Orsay {ECO:0000313|EMBL:CAB50141.1}; RX PubMed=11381026; DOI=10.1101/gr.GR1653R; RA Lecompte O., Ripp R., Puzos-Barbe V., Duprat S., Heilig R., Dietrich J., RA Thierry J.C., Poch O.; RT "Genome evolution at the genus level: comparison of three complete genomes RT of hyperthermophilic archaea."; RL Genome Res. 11:981-993(2001). RN [4] {ECO:0000313|EMBL:CAB50141.1, ECO:0000313|Proteomes:UP000000810} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GE5 / Orsay {ECO:0000313|Proteomes:UP000000810}, and Orsay RC {ECO:0000313|EMBL:CAB50141.1}; RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x; RA Cohen G., Barbe V., Flament D., Galperin M., Heilig R., Ripp R., RA Lecompte O., Prieur D., Poch O., Quellerou J., Thierry J.C., RA Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.; RT "An integrated analysis of the genome of the hyperthermophilic archaeon RT Pyrococcus abyssi."; RL Mol. Microbiol. 47:1495-1512(2003). RN [5] {ECO:0000313|EMBL:CCE70671.1, ECO:0000313|Proteomes:UP000009139} RP GENOME REANNOTATION. RC STRAIN=GE5 {ECO:0000313|EMBL:CCE70671.1}, and GE5 / Orsay RC {ECO:0000313|Proteomes:UP000009139}; RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x; RA Gao J., Wang J.; RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and RT Pyrococcus furiosus DSM 3638."; RL Curr. Microbiol. 64:118-129(2012). 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 --------------------------------------------------------------------------- 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; AJ248286; CAB50141.1; -; Genomic_DNA. DR EMBL; HE613800; CCE70671.1; -; Genomic_DNA. DR PIR; H75104; H75104. DR RefSeq; WP_010868348.1; NC_000868.1. DR AlphaFoldDB; Q9UZB8; -. DR STRING; 272844.PAB0819; -. DR GeneID; 1496617; -. DR KEGG; pab:PAB0819; -. DR PATRIC; fig|272844.11.peg.1314; -. DR eggNOG; arCOG00767; Archaea. DR HOGENOM; CLU_016950_7_1_2; -. DR OrthoDB; 10363at2157; -. DR Proteomes; UP000000810; Chromosome. DR Proteomes; UP000009139; Chromosome. 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}. FT DOMAIN 3..137 FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha" FT /evidence="ECO:0000259|Pfam:PF02878" FT DOMAIN 156..256 FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha" FT /evidence="ECO:0000259|Pfam:PF02879" FT DOMAIN 261..370 FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha" FT /evidence="ECO:0000259|Pfam:PF02880" FT DOMAIN 393..442 FT /note="Alpha-D-phosphohexomutase C-terminal" FT /evidence="ECO:0000259|Pfam:PF00408" SQ SEQUENCE 456 AA; 49943 MW; DBFA0FBAD4224A6F CRC64; MGKLFGTFGV RGIANEKITP EFTLKIGMAF GTLLKREGRE KPLVVVGRDT RVSGEMLKEA LISGLLSVGC DVIDVGIAPT PAIQWATKYF NADGGAVITA SHNPPEYNGI KLLEPNGMGL KKEREAIVEE LFFKEEFDRA KWYEIGEVRK EDIIKPYIEA IKSKVDVEAI KKRKPFVVVD TANGAGSLTL PYLLRELGCK VVTVNAQPDG HFPGRNPEPN EENLKEFIEI VKSLGADFGV AQDGDADRAV FIDEKGRFIQ GDKTFALVAD AVLRERGGGL LVTTVATSNL LDDIAKRNNA KVMRTKVGDL IVARTLFEHN GTIGGEENGG VIFPDHVLGR DGAMTVAKIV EIFAKSGKKF SELIDELPKY YQIKTKRHVE GDRHGIVNKV AEIARGRGYN VDTTDGAKII FEDGWVLVRA SGTEPIIRIF SEAKSEEKAK EYLNLGLGLL DEVLSS //