ID A8AAW5_IGNH4 Unreviewed; 456 AA.
AC A8AAW5;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:ABU82067.1};
DE EC=5.4.2.10 {ECO:0000313|EMBL:ABU82067.1};
GN OrderedLocusNames=Igni_0885 {ECO:0000313|EMBL:ABU82067.1};
OS Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignicoccus.
OX NCBI_TaxID=453591 {ECO:0000313|EMBL:ABU82067.1, ECO:0000313|Proteomes:UP000000262};
RN [1] {ECO:0000313|EMBL:ABU82067.1, ECO:0000313|Proteomes:UP000000262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIN4/I / DSM 18386 / JCM 14125
RC {ECO:0000313|Proteomes:UP000000262};
RX PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA Kyrpides N.C., Saier M.H.Jr., Richardson P.M., Rachel R., Huber H.,
RA Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT Nanoarchaeum equitans.";
RL Genome Biol. 9:R158.1-R158.18(2008).
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; CP000816; ABU82067.1; -; Genomic_DNA.
DR RefSeq; WP_012123031.1; NC_009776.1.
DR AlphaFoldDB; A8AAW5; -.
DR STRING; 453591.Igni_0885; -.
DR GeneID; 5562056; -.
DR KEGG; iho:Igni_0885; -.
DR eggNOG; arCOG00767; Archaea.
DR HOGENOM; CLU_016950_7_1_2; -.
DR OrthoDB; 10363at2157; -.
DR PhylomeDB; A8AAW5; -.
DR Proteomes; UP000000262; 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 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.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ABU82067.1};
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:UP000000262}.
FT DOMAIN 3..131
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 152..252
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 257..370
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 382..445
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 456 AA; 49578 MW; 119A4F1D5911F5DD CRC64;
MGRLFGTDGV RGITNEGMTP ELAMKVAQAA CTWLGGGKVL VGRDVRYGGD MLVSAVLAGL
SSCGCEPYYA GLVPTPALQY AVPRLGYDMG IMVTASHNPP QYNGVKVIGS NGVEVPRDAE
REIEEIIFEN KVRRVPYYEV KEAKREGRVL DVYIDGILAD IDVQKVKNKE FKVVVDGANS
VGSLATPLVL RKLGAKVLCL NCNLDPSFPG RHPEPTPQSL EETSRAAVAV GADLIVAHDA
DADRAIIGDE AGEVHWGDRS GALLTEHLAE KYPHLPKRTF TGVSSSHIVV DGYLRPKGIE
VVWTPVGSVV IAHELIKRGG VSGFEENGGF MNPVHQPVRD GAMTAALFLE MLAQRGKRAS
ELFSALPKAY AIKGKVYRGE KEELRGLYEA LKSKYQDCQF TEIDGLKVVC ENFWFLVRPS
GTEPVVRIMV EATDPKKAKE VYSELESFVK AFLGST
//
