ID A0A1J0AEX7_9CYAN Unreviewed; 838 AA.
AC A0A1J0AEX7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Nucleotidyl transferase {ECO:0000313|EMBL:APB34477.1};
DE EC=2.7.7.13 {ECO:0000313|EMBL:APB34477.1};
GN ORFNames=GlitD10_2148 {ECO:0000313|EMBL:APB34477.1};
OS Gloeomargarita lithophora Alchichica-D10.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gloeomargaritales;
OC Gloeomargaritaceae; Gloeomargarita.
OX NCBI_TaxID=1188229 {ECO:0000313|EMBL:APB34477.1, ECO:0000313|Proteomes:UP000180235};
RN [1] {ECO:0000313|EMBL:APB34477.1, ECO:0000313|Proteomes:UP000180235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D10 {ECO:0000313|EMBL:APB34477.1,
RC ECO:0000313|Proteomes:UP000180235};
RA Moreira D., Tavera R., Benzerara K., Skouri-Panet F., Couradeau E.,
RA Gerard E., Loussert C., Novelo E., Zivanovic Y., Lopez-Garcia P.;
RT "Description of Gloeomargarita lithophora gen. nov., sp. nov., a thylakoid-
RT bearing basal-branching cyanobacterium with intracellular carbonates, and
RT proposal for Gloeomargaritales ord. nov.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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DR EMBL; CP017675; APB34477.1; -; Genomic_DNA.
DR RefSeq; WP_071454907.1; NZ_CP017675.1.
DR AlphaFoldDB; A0A1J0AEX7; -.
DR STRING; 1188229.GlitD10_2148; -.
DR OrthoDB; 9803871at2; -.
DR Proteomes; UP000180235; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProt.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
DR GO; GO:0043886; F:structural constituent of carboxysome shell; IEA:UniProt.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05805; MPG1_transferase; 1.
DR CDD; cd04181; NTP_transferase; 1.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 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; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR22572:SF15; MANNOSE-1-PHOSPHATE GUANYLTRANSFERASE BETA; 1.
DR PANTHER; PTHR22572; SUGAR-1-PHOSPHATE GUANYL TRANSFERASE; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 2.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000313|EMBL:APB34477.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000180235};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:APB34477.1}.
FT DOMAIN 3..230
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 383..514
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 534..631
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 641..742
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 838 AA; 91389 MW; 0C9A5097FD4C3C51 CRC64;
MRAVLMAGGA GTRLRPLTCD LPKPLMPVLN RPIAEHTLAW LRGHGLTELI MTLHYLPDMV
QSYFQDGREF GVQLSYVVEE LRPLGTAGGV RQVAALLPET FVVVSGDVIT DGNLQAAIGF
HRERGAKMTV ILTQVPDPGE FGVVITDGDG RVVRLLEKPT PGEVFSDRVN TGAYIVEPEI
LAYLAPDQPA DFAQDLLPQL LAAGEPVYGF VSGGYWCDVG NLERYRQVQW DALTGRVRLA
SAYRQVQTGV WLGEQVRLDP SVVWEPPVLI GHHCRIGAGV RLGAGTVIGD HVTVGAQADL
KRPVLFNGVM VGEESHLRAC VVGRGSRIGR RVQILEGAVL GHLCTVGEEA QVQSGCRIWP
GKYIEPGATV HTNLIWGTGA RRHLFGARGV AGLANVDITP ELAIRLGAAF GSCLAPGAQV
QVSRDQRKVS RMISRSIISG LMSVGVQVQN LEANAIPISR LVGRVLGVDG GVHVRLDPDQ
AGHVLIEFLD NQGINIPPTL EKKIEATLIR EEFRRAALAD IGDMTVPGRV ADIYRGAFQQ
QLHVEAIRQS RAKVVVDYAH GVSGAVLPEL LVGYGCDPLV LNASLRQTPL SAEERESLLQ
QLGRVVEAVR AHLGVQVNAN GERLVLVDET GTAMQGSLLT AVVMELILAG QGRGTVAVPV
TTSSLVEQVA RYHEGRVLRT KANATALMRI GQDQPRILCA GSGELGFIFP QLHPGFDAMF
TIAKILELLT VQERSLAQIR THLPSVVWKT QTIHCPWRLK GAWMRHLVET HTPDALDLTD
GVRIFPQGYD PDHWVLFLPD ATEPLLHLVV NGLEREWVTH WGQTYRQRLQ EFMEQSEV
//
