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Database: UniProt
Entry: M1WUT6_PSEP2
LinkDB: M1WUT6_PSEP2
Original site: M1WUT6_PSEP2 
ID   M1WUT6_PSEP2            Unreviewed;       476 AA.
AC   M1WUT6;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   Name=algA {ECO:0000313|EMBL:CCH47853.1};
GN   OrderedLocusNames=BN4_10616 {ECO:0000313|EMBL:CCH47853.1};
OS   Pseudodesulfovibrio piezophilus (strain DSM 21447 / JCM 15486 / C1TLV30)
OS   (Desulfovibrio piezophilus).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae.
OX   NCBI_TaxID=1322246 {ECO:0000313|EMBL:CCH47853.1, ECO:0000313|Proteomes:UP000011724};
RN   [1] {ECO:0000313|EMBL:CCH47853.1, ECO:0000313|Proteomes:UP000011724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011724};
RX   PubMed=23383081; DOI=10.1371/journal.pone.0055130;
RA   Pradel N., Ji B., Gimenez G., Talla E., Lenoble P., Garel M., Tamburini C.,
RA   Fourquet P., Lebrun R., Bertin P., Denis Y., Pophillat M., Barbe V.,
RA   Ollivier B., Dolla A.;
RT   "The first genomic and proteomic characterization of a deep-sea sulfate
RT   reducer: insights into the piezophilic lifestyle of Desulfovibrio
RT   piezophilus.";
RL   PLoS ONE 8:e55130-e55130(2013).
RN   [2] {ECO:0000313|Proteomes:UP000011724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011724};
RX   PubMed=23961312; DOI=10.4056/sigs.3777412;
RA   Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA   Schreiber L.;
RT   "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT   deltaproteobacterium specialized in disproportionating inorganic sulfur
RT   compounds.";
RL   Stand. Genomic Sci. 8:58-68(2013).
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; FO203427; CCH47853.1; -; Genomic_DNA.
DR   RefSeq; WP_015413907.1; NC_020409.1.
DR   AlphaFoldDB; M1WUT6; -.
DR   STRING; 1322246.BN4_10616; -.
DR   KEGG; dpi:BN4_10616; -.
DR   PATRIC; fig|879567.3.peg.641; -.
DR   eggNOG; COG0662; Bacteria.
DR   eggNOG; COG0836; Bacteria.
DR   HOGENOM; CLU_035527_1_0_7; -.
DR   OrthoDB; 9806359at2; -.
DR   BioCyc; DPIE1322246:BN4_RS03165-MONOMER; -.
DR   Proteomes; UP000011724; 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:CCH47853.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:CCH47853.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011724};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCH47853.1}.
FT   DOMAIN          17..290
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          319..469
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   476 AA;  53408 MW;  1EE8EC680DA12146 CRC64;
     MQKNRPLKAQ FAEECHAIIL AGGSGTRLWP LSRNLLPKQL LVLDGEQTLL QQSVARVLEL
     FDPEKIWVVT NDEHVFEVRK QIAEICPNME TQVLSEPVGR NTLPAIMLGL DKVVEANPRA
     QAAIFPSDHL IGNCQAWGED IVQASCLAAE KLFVTFGVKP RTPETGYGYI TLGKKICDDA
     FAVDGFVEKP GLEKAEAFLR EGSHFWNSGM FLFRAKDFLT QVAKFQPDLW DWWMERDQTS
     LVQGYRELPN ISVDYGVVEK IDNIAVVRAQ FDWDDLGSWE ALYRIGEKDQ NGNVIQGDVL
     AMDCHNSLLI SEGGKLAVVG VENMIMVQTR DATLSCPMEH VQSVRDVVAT LKAEGSRLVE
     SHPTVVRPWG SYSVLEEGPH YKIKRIQVNP GARLSSQMHH HRSEHWVVVD GTAEVEVDEK
     PVILVENQSI DIPKASQHRL ANPGKVPLNI IEIQSGPYLE EDDIVRFDDV YGRVQK
//
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