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Database: UniProt
Entry: Q07IN7_RHOP5
LinkDB: Q07IN7_RHOP5
Original site: Q07IN7_RHOP5 
ID   Q07IN7_RHOP5            Unreviewed;       470 AA.
AC   Q07IN7;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   OrderedLocusNames=RPE_4272 {ECO:0000313|EMBL:ABJ08197.1};
OS   Rhodopseudomonas palustris (strain BisA53).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316055 {ECO:0000313|EMBL:ABJ08197.1};
RN   [1] {ECO:0000313|EMBL:ABJ08197.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisA53 {ECO:0000313|EMBL:ABJ08197.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL   Submitted (SEP-2006) 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; CP000463; ABJ08197.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q07IN7; -.
DR   STRING; 316055.RPE_4272; -.
DR   KEGG; rpe:RPE_4272; -.
DR   eggNOG; COG0662; Bacteria.
DR   eggNOG; COG0836; Bacteria.
DR   HOGENOM; CLU_035527_1_0_5; -.
DR   OrthoDB; 9806359at2; -.
DR   GO; GO:0005525; F:GTP binding; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:ABJ08197.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABJ08197.1}.
FT   DOMAIN          7..286
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          316..465
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   470 AA;  51133 MW;  D1D43F83D8765F88 CRC64;
     MTSPIIPLIM CGGAGTRLWP ASREVLPKQF LPLFGPRSTF QDTLLRVSDP ELFGRAIIIT
     NLAYRFMVLE QLAEIGLSAD VLLEPARRDS GPAIAAGAAF AQTRDPDAIV LALAADHVVT
     DTPAFVAACR EGLAAAETGS IVTFGVEPSR PATEYGYIRP GDAVVGRVRK VASFVEKPDP
     ATAAAYIKDG YLWNSGNFMF RASVLLDEYR AVDPASVQTI IAAVEKAGRD LGFVTLDPPA
     FEQAKPISVD YAVMEKTGLA AVVPVACGWS DVGSWHAVWE LSAKDEHGNA ARGEAVFEDS
     RNCNVTTDKT LVALEGVDDL VVVATQDAVL VSRQKDANGL KRLVSKLKAV APQLTESHVR
     VHRPWGSYES LDNGDRHQVK RIVVKAGGRL SLQLHHHRSE HWIVVRGTAR VIIDDLDKIL
     HENESIYIPI GATHRLENPG KIPLELIEVQ TGSYLGEDDI VRIEDDYRRS
//
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