ID A2SR83_METLZ Unreviewed; 419 AA.
AC A2SR83;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:ABN06839.1};
DE EC=5.4.2.10 {ECO:0000313|EMBL:ABN06839.1};
GN OrderedLocusNames=Mlab_0667 {ECO:0000313|EMBL:ABN06839.1};
OS Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX NCBI_TaxID=410358 {ECO:0000313|EMBL:ABN06839.1, ECO:0000313|Proteomes:UP000000365};
RN [1] {ECO:0000313|EMBL:ABN06839.1, ECO:0000313|Proteomes:UP000000365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43576 / DSM 4855 / Z {ECO:0000313|Proteomes:UP000000365};
RX PubMed=21304657; DOI=10.4056.sigs.35575;
RA Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL Stand. Genomic Sci. 1:197-203(2009).
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; CP000559; ABN06839.1; -; Genomic_DNA.
DR RefSeq; WP_011833040.1; NC_008942.1.
DR AlphaFoldDB; A2SR83; -.
DR STRING; 410358.Mlab_0667; -.
DR GeneID; 4794889; -.
DR KEGG; mla:Mlab_0667; -.
DR eggNOG; arCOG00767; Archaea.
DR HOGENOM; CLU_016950_7_1_2; -.
DR OrthoDB; 10363at2157; -.
DR Proteomes; UP000000365; 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: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 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:ABN06839.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000365}.
FT DOMAIN 2..120
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 154..237
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 241..326
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 359..407
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 419 AA; 45159 MW; CF25F53827FFC4A1 CRC64;
MLFGSSGIRQ LFDQHLLSLA PIVGAAVAKN AKHVVLGTDS RTSRNVLAHA VISGLISGGA
DVVYGGICPT PTVAFGAGFA DAGVMITASH NPEPYNGIKL FRSDGSSYTL AQQKEIEEEV
DCPVWSSWDE QGSFTDADLI TPHKEAILTS VCIPEDITIV VDCGNGAGGQ ITPKLFEESG
TAVIPVNCDP SGKFARPSEP LEKNLLHIPK LMKKINADCA VVNDGDADRM MAFDNLGRYI
DGDHLLMLFA KYLDAKQVVT TVDASMAIEE IAEVRRTPVG DSFVSEELIS WGTFGGEPSG
SWIFPKHSLC PDGPYAAALF AEISGEWNVA EELDAMPRYT ILRDALETKN AKEILSGLGA
DKPTDGIRIS DENGWCLIRA SGTEPKIRCT AEGRTKDDAK RMLESGMNKI RDSMHQIRE
//
