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Database: UniProt
Entry: A0A1I6LX36_9GAMM
LinkDB: A0A1I6LX36_9GAMM
Original site: A0A1I6LX36_9GAMM 
ID   A0A1I6LX36_9GAMM        Unreviewed;       470 AA.
AC   A0A1I6LX36;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   ORFNames=SAMN05216570_2337 {ECO:0000313|EMBL:SFS07968.1};
OS   Dyella sp. OK004.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=1855292 {ECO:0000313|EMBL:SFS07968.1, ECO:0000313|Proteomes:UP000198834};
RN   [1] {ECO:0000313|EMBL:SFS07968.1, ECO:0000313|Proteomes:UP000198834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK004 {ECO:0000313|EMBL:SFS07968.1,
RC   ECO:0000313|Proteomes:UP000198834};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC       biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00004823}.
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; FOZI01000002; SFS07968.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6LX36; -.
DR   STRING; 1855292.SAMN05216570_2337; -.
DR   OrthoDB; 9806359at2; -.
DR   UniPathway; UPA00126; UER00930.
DR   Proteomes; UP000198834; 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:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
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:SFS07968.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:SFS07968.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198834};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SFS07968.1}.
FT   DOMAIN          4..282
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          315..465
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   470 AA;  51722 MW;  81352A09A6B5682C CRC64;
     MLIPLILSGG SGTRLWPVSR KNLPKQFLSL TGAGTLFQQT VTRTRMLSRV AAPIIVASED
     HRFLAAEQLL ELGIKEASIM LEPVARNTAP AIALGALHAL ATDPEAILLV LPADHLIGDE
     RSFVEAVQLA LPTAEAGWLV TFGIRPDRPE TGFGYIRRAE VIDKNAYRVE QFVEKPNLVK
     AESYLADGGY DWNSGMFLFK ASSYLEELAE HAPEILGAVR VAYATAKSDL DFVRIDESAF
     SKVPDNSIDY AVMEKCRRAA VIPVTCDWSD IGSWSALWLA GLRDADGNLR EGDTIAVNTA
     NSLLRSHDRH LLATVGVNDL IVVTTPDATL VAHRNAAQDV KRVVDELKTA GRTEHSLHRI
     VRRPWGSYDS LEAGERFQVK RIVVKPGAAL SLQKHHHRAE HWIVVSGTAE VTCDDKVFTL
     SENQSTYIPL GSVHRLRNPG KMPLEIIEVQ SGSYLGEDDI VRLEDVYGRS
//
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