ID   A0A1W6SL65_9PROT        Unreviewed;       482 AA.
AC   A0A1W6SL65;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   ORFNames=EBAPG3_001400 {ECO:0000313|EMBL:ARO86545.1};
OS   Nitrosospira lacus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=1288494 {ECO:0000313|EMBL:ARO86545.1, ECO:0000313|Proteomes:UP000012179};
RN   [1] {ECO:0000313|EMBL:ARO86545.1, ECO:0000313|Proteomes:UP000012179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APG3 {ECO:0000313|EMBL:ARO86545.1,
RC   ECO:0000313|Proteomes:UP000012179};
RX   PubMed=25336720; DOI=10.1099/ijs.0.070789-0;
RA   Urakawa H., Garcia J.C., Nielsen J.L., Le V.Q., Kozlowski J.A., Stein L.Y.,
RA   Lim C.K., Pommerening-Roser A., Martens-Habbena W., Stahl D.A., Klotz M.G.;
RT   "Nitrosospira lacus sp. nov., a psychrotolerant, ammonia-oxidizing
RT   bacterium from sandy lake sediment.";
RL   Int. J. Syst. Evol. Microbiol. 65:242-250(2015).
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; CP021106; ARO86545.1; -; Genomic_DNA.
DR   RefSeq; WP_004180921.1; NZ_CP021106.3.
DR   AlphaFoldDB; A0A1W6SL65; -.
DR   KEGG; nlc:EBAPG3_001400; -.
DR   eggNOG; COG0662; Bacteria.
DR   eggNOG; COG0836; Bacteria.
DR   OrthoDB; 9806359at2; -.
DR   Proteomes; UP000012179; Chromosome.
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:ARO86545.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:ARO86545.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012179};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ARO86545.1}.
FT   DOMAIN          6..296
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          325..475
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   482 AA;  52807 MW;  9ECF45224E076171 CRC64;
     MSLLIPVVLS GGSGTRLWPL SREKYPKQLL PLIGEDSLLQ ATVRRMEGLA DIELGAPLVV
     CNEEYRFVIA EQLRLIGMKG TLLLEPAGRN TAPALTLAAL ATMREGGDPI LLVMPADHVI
     ADTKCFQAAV RKGMTLAAEG AVVTFGIKPD SPETGYGYIQ SGDPIDPDGT CRIARFVEKP
     DLATAEAYLD AGSYFWNSGL FMLRASVWLS AIGFCRPDIL AACRAAWDKG SIDGDFLRVN
     REAFMQCPSD SIDYAVMERI AAGEGSLPIG AVIPLSAGWS DVGAWDSLWE VLPKDQRGNV
     SQGDVMLHDC NNMLVMSEDR LVACVGVDDM VVVETPDAIL VAHMSRTQDV KKIVDSLKRE
     GRPEGQLHRK VFRPWGWYDG VDAGERFQVK RIVVKPGAAL SLQMHHHRAE HWIVVRGTAQ
     VTRGDASYLV SENESTFIPL GTRHRLENPG CLPLEMIEVQ SGSYLGEDDI VRFEDVYGRK
     EG
//