ID A0A0V0ZIB5_9BILA Unreviewed; 893 AA.
AC A0A0V0ZIB5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=phosphoacetylglucosamine mutase {ECO:0000256|ARBA:ARBA00012731};
DE EC=5.4.2.3 {ECO:0000256|ARBA:ARBA00012731};
DE AltName: Full=Acetylglucosamine phosphomutase {ECO:0000256|ARBA:ARBA00032065};
DE AltName: Full=N-acetylglucosamine-phosphate mutase {ECO:0000256|ARBA:ARBA00031926};
GN Name=ATAD1 {ECO:0000313|EMBL:KRY12165.1};
GN ORFNames=T12_10270 {ECO:0000313|EMBL:KRY12165.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY12165.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY12165.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY12165.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-
CC glucosamine 6-phosphate; Xref=Rhea:RHEA:23804, ChEBI:CHEBI:57513,
CC ChEBI:CHEBI:57776; EC=5.4.2.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000558};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from
CC alpha-D-glucosamine 6-phosphate (route I): step 2/2.
CC {ECO:0000256|ARBA:ARBA00004865}.
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:KRY12165.1}.
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DR EMBL; JYDQ01000172; KRY12165.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0ZIB5; -.
DR STRING; 990121.A0A0V0ZIB5; -.
DR UniPathway; UPA00113; UER00530.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004610; F:phosphoacetylglucosamine mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03086; PGM3; 1.
DR Gene3D; 1.10.8.60; -; 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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR049023; AMG1_II.
DR InterPro; IPR049022; AMG1_III.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016657; PAGM.
DR PANTHER; PTHR45955; PHOSPHOACETYLGLUCOSAMINE MUTASE; 1.
DR PANTHER; PTHR45955:SF1; PHOSPHOACETYLGLUCOSAMINE MUTASE; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF21405; AMG1_II; 1.
DR Pfam; PF21404; AMG1_III; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR PROSITE; PS00674; AAA; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000054783}.
FT DOMAIN 116..256
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 893 AA; 101235 MW; 92E77E7ABA23A09D CRC64;
MDGRPSWNMF AAQLARLIIG SVISYFTAKL IVRQFDQTTA KKEQTKKKAE RICNILGIQV
QDLDEYEMRI ATQLVNPKDC SVSWSDVGGY SNLISELREN IIFPLCTSIK SKHFSAPKGV
LLHGPPGCGK TMMVKAIAKE AGANFINLEI SEMIDKWCGE TEKMTTALFS FAKKIQPTII
FIDEIDSFLR HRQSRDHEMT AMMKALFLSH WDGFFSESEL RVVIIGATNR PKDVDSAILR
RMPLRFCIRH PNLQQRCDIL TTMLRSESLS QDVNLFEIAN HSCGFSCSDL VELCRVADII
RVRESLKQDQ EIKQENSFSE QVEIRPFEQS DFLKAVERMN KDNEDMLLNR HDEIELMMRF
NVESIPPECR QSHRMNRVYG TAGFRDDANT LKCVMYRMGL LACLRSQQTG MVVGVMITAS
HNPAKDNGVK IIDPMGDMLA PEWEKHATEI ANCSDDQLIS TLEMIVSKNN ICISAEASVF
CAHDNRESST VLYNVLKSGV DVMSGKFILF GMLTTPQLHF IVRHGNCFKN YDPVFLENFY
YEEVTKAFKN VNTSMQQSCK AYNPNVFIDC GNGVGGKAMR FFVENLKPLL NIILVNQSNH
HLNDKCGADF VKIEQQIPTV YDANLRIIPG QRWASFDGDA DRIVYFYLDS KRVFHILDGD
KIAVLMVSFV LDLIQKGNLR TSIGVVQTAF ANGSSTRYIE DVLKIPVVIT ETGVKHLHKE
AKKFDIGIYF EANGHGTVLF SERMVDELQK HLELISAECA EARRTLSNLV HLINQANGDA
MTNLLLAETI LQHRDWNIEK WDEMFVDYPC RQLKIKVSNR FAVKTADCDR ICVAPSGLWE
RITELGKKYS YSRAFIRPSG TEDVVRVYAE AGKQEDADDL AALIGKAVQE FVG
//
