ID A0A498DF04_9PROT Unreviewed; 454 AA.
AC A0A498DF04;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
DE Flags: Fragment;
GN ORFNames=D8Y20_07585 {ECO:0000313|EMBL:RLL52252.1};
OS Mariprofundus sp. EBB-1.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=2650971 {ECO:0000313|EMBL:RLL52252.1, ECO:0000313|Proteomes:UP000270267};
RN [1] {ECO:0000313|Proteomes:UP000270267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EBB-1 {ECO:0000313|Proteomes:UP000270267};
RA Lopez A., Barco R., Canela R., Emerson D., Tully B., Abuyen K.,
RA Broomell S., Albino D., Beraki S., Dingmon T., Estrada S., Fernandez M.,
RA Amend J.;
RT "Genome Sequence of Zetaproteobacterium sp. EBB-1: a novel, marine, iron-
RT oxidizing chemolithoautotroph isolated from an iron-sulfide mineral.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-
CC alpha-D-mannose; Xref=Rhea:RHEA:15229, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57527,
CC ChEBI:CHEBI:58409; EC=2.7.7.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001083};
CC -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 2 family.
CC {ECO:0000256|ARBA:ARBA00006115, ECO:0000256|RuleBase:RU004190}.
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:RLL52252.1}.
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; RCFQ01000014; RLL52252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498DF04; -.
DR Proteomes; UP000270267; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
DR CDD; cd02213; cupin_PMI_typeII_C; 1.
DR CDD; cd02509; GDP-M1P_Guanylyltransferase; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR049577; GMPP_N.
DR InterPro; IPR006375; Man1P_GuaTrfase/Man6P_Isoase.
DR InterPro; IPR001538; Man6P_isomerase-2_C.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR NCBIfam; TIGR01479; GMP_PMI; 1.
DR PANTHER; PTHR46390; MANNOSE-1-PHOSPHATE GUANYLYLTRANSFERASE; 1.
DR PANTHER; PTHR46390:SF1; MANNOSE-1-PHOSPHATE GUANYLYLTRANSFERASE; 1.
DR Pfam; PF01050; MannoseP_isomer; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Isomerase {ECO:0000313|EMBL:RLL52252.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:RLL52252.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000270267};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RLL52252.1}.
FT DOMAIN 6..284
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 313..454
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
FT NON_TER 454
FT /evidence="ECO:0000313|EMBL:RLL52252.1"
SQ SEQUENCE 454 AA; 50230 MW; F9AB7743F5F80E1F CRC64;
MSDRLKAVVL AGGSGSRLWP LSRQQLPKQF LNLNGHESML GATINRLSPL IERDNVWVVT
GEKHATGEAF SELDGLNTML EPCGRNTAPA VALSAALMQD LYDDDPIMVV LPADHIISKK
DAFQACLQQA VEAAKAGRLV TFGIFPNQPE TGFGYVQTEE SVDGIHRVLR FVEKPNKEKA
QKMLDDGNYY WNSGMFVWRA SVILAEVEKY LPDVWAVLQD MRKRWNSGEV WQEVVRTRFD
QMPDISIDYG VMERSEIVSL VSADIGWSDV GSWDAVHEIA TNDTDGNEIS GNVLAIDCKN
SLFRSESRLI AAVGLDDMIV VETPDAILLA KAGESQRVRE LVDSLKLGGE KYHIEHVTVR
RPWGSYTVLG ESGDGYQLKR ITVLPGAKLS LQAHQHRSEH WVVVAGTATV TCGDLVKVVA
RNGSAYIPIG EVHRLENRGK VPVQLIEVQV GDYL
//
