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Database: UniProt
Entry: M1P9J3_DESSD
LinkDB: M1P9J3_DESSD
Original site: M1P9J3_DESSD 
ID   M1P9J3_DESSD            Unreviewed;       469 AA.
AC   M1P9J3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   OrderedLocusNames=UWK_01769 {ECO:0000313|EMBL:AGF78327.1};
OS   Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfocapsaceae; Desulfocapsa.
OX   NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF78327.1, ECO:0000313|Proteomes:UP000011721};
RN   [1] {ECO:0000313|Proteomes:UP000011721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
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; CP003985; AGF78327.1; -; Genomic_DNA.
DR   RefSeq; WP_015404018.1; NC_020304.1.
DR   AlphaFoldDB; M1P9J3; -.
DR   STRING; 1167006.UWK_01769; -.
DR   KEGG; dsf:UWK_01769; -.
DR   PATRIC; fig|1167006.5.peg.1951; -.
DR   eggNOG; COG0662; Bacteria.
DR   eggNOG; COG0836; Bacteria.
DR   HOGENOM; CLU_035527_1_0_7; -.
DR   OMA; CRRNTAP; -.
DR   OrthoDB; 9806359at2; -.
DR   Proteomes; UP000011721; Chromosome.
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; 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:AGF78327.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:AGF78327.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011721};
KW   Transferase {ECO:0000313|EMBL:AGF78327.1}.
FT   DOMAIN          6..284
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          313..463
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   469 AA;  52433 MW;  DC1CB70F9E269269 CRC64;
     MSKIQPIILA GGTGSRLWPL SRELYPKQLL NLIDETSLLQ TTVLRVAQLT EVLPPLLVVG
     EEHRFITRSQ VDCLGGGGVC DILLEPVGRN TAPAVCGAVE YCAVSLPEDT ILLVLPADHL
     ILRKAVFQEV VAEAVRLAVE GKIVTFGIEP QHPETGYGYI EKGEGSSVRS FREKPDYETA
     KSYLEKGNYL WNSGMFAFSI KTFREEMERL APEMVSCMRE SVLLGKRDGS FFRLDEAAMS
     RSPSDSIDYA LMEKTDRAAV VAADLDWSDI GSWHALWEVS AKDKDGNVTK GDVILEDTKN
     CLIRSEDTLV ATVGLEDILV VETSDAVLVA PLSRAQDVKK IVARLKKDSR SEFKLHRTVY
     RPWGSYTVLE QHERYQIKRI TVSPGSKLSL QMHHHRHEHW VVVSGTARIT NGEKVFLLYE
     NQSTYIPAGV NHRLENPGVM DLELIEVQNG SYLGEDDIVR FEDDYGRGE
//
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