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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//