ID   NOEJ_SINFN              Reviewed;         512 AA.
AC   P55357;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Mannose-1-phosphate guanylyltransferase;
DE            EC=2.7.7.13;
DE   AltName: Full=GDP-mannose pyrophosphorylase;
DE            Short=GMP;
DE            Short=GMPP;
GN   Name=noeJ; OrderedLocusNames=NGR_a00380; ORFNames=y4aJ;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234a.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=9163424; DOI=10.1038/387394a0;
RA   Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA   Perret X.;
RT   "Molecular basis of symbiosis between Rhizobium and legumes.";
RL   Nature 387:394-401(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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   -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 2 family.
CC       {ECO:0000305}.
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; U00090; AAB91607.1; -; Genomic_DNA.
DR   RefSeq; NP_443769.1; NC_000914.2.
DR   AlphaFoldDB; P55357; -.
DR   SMR; P55357; -.
DR   KEGG; rhi:NGR_a00380; -.
DR   PATRIC; fig|394.7.peg.36; -.
DR   eggNOG; COG0662; Bacteria.
DR   eggNOG; COG0836; Bacteria.
DR   HOGENOM; CLU_035527_1_0_5; -.
DR   OrthoDB; 9806359at2; -.
DR   Proteomes; UP000001054; Plasmid sym pNGR234a.
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; Nodulation; Nucleotide-binding; Nucleotidyltransferase;
KW   Plasmid; Reference proteome; Transferase.
FT   CHAIN           1..512
FT                   /note="Mannose-1-phosphate guanylyltransferase"
FT                   /id="PRO_0000194263"
SQ   SEQUENCE   512 AA;  56213 MW;  6D89C7C4D7F61FFE CRC64;
     MNSHPLMRLL RSRHTVMKLP SNAIKNDTML PKIIPAIMAG GRGTRLWPLS RATAAKQFLK
     LIGEETLFQD TLKRVSDAKV YGAPLVITNE EFRFLVAEQA RELGVTLSSI VLEPVPRNTA
     AAVAVAARIV ADRFGEDALL LVLPSDHAIT VDDTYKKCVR SACIAAAEGK LVTFGIQPTW
     PATGYGYIER GTYLGKDVHA VQCFVEKPSL EKAAALLETG NYYWNSGMFL FQAASIIAEL
     EEHAPDVLSA VHAAVRGSTV DADFIRLAPE SFSQAPSISI DYALMEKTAN AAVVCSDFAW
     SDLGSWDAVW KNEEQNADGN VLKGNVTACN TKNSLVLSHT AHLAVQGMDG VAVIASEDAV
     FVGRLEEAHE IGNLVKRLAA DENTARLTEL HPTLIRPWGG YTTMLNGDRF QVRRLFVRPG
     KMLSLHKHFH RSEHWICVKG TAEVTIEDRV TILHENQSIY IPEGAIHRLG NPGKIMLELV
     EIQTGAYLGE DDIIRVADES RNEMPDSRRT GP
//