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Database: UniProt
Entry: A0A1X7JRH6_9BACT
LinkDB: A0A1X7JRH6_9BACT
Original site: A0A1X7JRH6_9BACT 
ID   A0A1X7JRH6_9BACT        Unreviewed;       461 AA.
AC   A0A1X7JRH6;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   ORFNames=SAMN06275492_11466 {ECO:0000313|EMBL:SMG30118.1};
OS   Dethiosulfovibrio salsuginis.
OC   Bacteria; Synergistota; Synergistia; Synergistales;
OC   Dethiosulfovibrionaceae; Dethiosulfovibrio.
OX   NCBI_TaxID=561720 {ECO:0000313|EMBL:SMG30118.1, ECO:0000313|Proteomes:UP000193355};
RN   [1] {ECO:0000313|EMBL:SMG30118.1, ECO:0000313|Proteomes:UP000193355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USBA 82 {ECO:0000313|EMBL:SMG30118.1,
RC   ECO:0000313|Proteomes:UP000193355};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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}.
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DR   EMBL; FXBB01000014; SMG30118.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7JRH6; -.
DR   STRING; 561720.SAMN06275492_11466; -.
DR   OrthoDB; 9806359at2; -.
DR   Proteomes; UP000193355; 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:SMG30118.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          10..281
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          312..461
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   461 AA;  51040 MW;  437FCDBA16A29DCC CRC64;
     MNNDIKKLRA LILAGGGGTR LWPLSREEVP KQFLKLAGDQ SLLQTTIKRL LPLCGQEGIK
     IVAGERWDSQ IAYQASDVGL KGDILVLEPE GKNTAPAIAL GLAHLMEKGA TRETPVLVCP
     SDHIIQNEKA FHDALKLGLL ALEEGKLVTF GIVPDAPETG FGYIKKGEDR GGWHDVSQFV
     EKPDLKKATE YIQSGQYLWN GGIFLFRAGD MIDSFKEHLP EIARLMECGE RAMVEGFKDL
     PSVSIDYGIM EKAPSVAVVP LDACWSDLGS WDAIYQQGEK DGNRNVLKGD VLADRSEGCL
     VQGDRRLIAL SGVSDLLVVD TADALFIAPR GTSQSVKDVV STLKERSRPE ITQAPESARR
     WGDYRILHEG DGIKVKRITV HPGKALSLQY HHHRTEHWIV VKGTAQVERD GETFYLHEGE
     STFIQKNQLH RLINPGKISL EIIEVQNGPY LGEDDIFRVE E
//
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