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Database: UniProt
Entry: A9BD48_PROM4
LinkDB: A9BD48_PROM4
Original site: A9BD48_PROM4 
ID   A9BD48_PROM4            Unreviewed;       482 AA.
AC   A9BD48;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   Name=manC {ECO:0000313|EMBL:ABX09661.1};
GN   OrderedLocusNames=P9211_17301 {ECO:0000313|EMBL:ABX09661.1};
OS   Prochlorococcus marinus (strain MIT 9211).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=93059 {ECO:0000313|EMBL:ABX09661.1, ECO:0000313|Proteomes:UP000000788};
RN   [1] {ECO:0000313|EMBL:ABX09661.1, ECO:0000313|Proteomes:UP000000788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9211 {ECO:0000313|Proteomes:UP000000788};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000878; ABX09661.1; -; Genomic_DNA.
DR   RefSeq; WP_012196281.1; NC_009976.1.
DR   AlphaFoldDB; A9BD48; -.
DR   STRING; 93059.P9211_17301; -.
DR   KEGG; pmj:P9211_17301; -.
DR   eggNOG; COG0662; Bacteria.
DR   eggNOG; COG0836; Bacteria.
DR   HOGENOM; CLU_035527_1_0_3; -.
DR   OrthoDB; 9806359at2; -.
DR   Proteomes; UP000000788; Chromosome.
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:ABX09661.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000788};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABX09661.1}.
FT   DOMAIN          8..294
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          323..473
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   482 AA;  54454 MW;  79B822E50540F4F2 CRC64;
     MTDRPLIPVI LCGGSGTRLW PLSRASYPKQ YWSLCGNENE SLLQQTHKRL EGLPELEQPL
     LICHEEHRFI VAEQMREINI EPKEIILEPV GRNTAAAIAV AAIKATESGE DPQLLVLSAD
     HEIRNVEEFQ KSIAAGRIEA QKGKLITFGI IPTCAETGYG YIQAKEPIDH SNPKAVKINK
     FFEKPTQEKA EEFIANPCFS WNSGMFLFQA STILKELEKL APKILKSCKS ALQGELSDLD
     FLRLEKKAFS ECPNLSIDIA VMEKTNLGTV LPLNAGWNDV GNWHSLWETA SKDSNGNFSK
     GKVIIKRSKN CYFRSEHRLI VGLGVEDLIL IETDDAVLVT NQKDAQSVKD IVNELEHKKL
     SESKAHRKIY RPWGHYTSIV EGKRWQVKRI EVKPGEFLSL QMHHHRAEHW VIVKGTALIE
     RDGKEELLGE NQSTYIPLGC KHRLGNPGKM PLELIEIQSG AYIGEDDILR LEDRYGRVNK
     NK
//
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