NOEJ_SINFN
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 25-MAY-2022, entry version 127.
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; Proteobacteria; 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}.
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DR EMBL; U00090; AAB91607.1; -; Genomic_DNA.
DR RefSeq; NP_443769.1; NC_000914.2.
DR AlphaFoldDB; P55357; -.
DR SMR; P55357; -.
DR STRING; 394.NGR_a00380; -.
DR EnsemblBacteria; AAB91607; AAB91607; NGR_a00380.
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 OMA; ELKKHDP; -.
DR OrthoDB; 224217at2; -.
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 activity; IEA:UniProtKB-EC.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
DR Gene3D; 2.60.120.10; -; 1.
DR Gene3D; 3.90.550.10; -; 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 Pfam; PF01050; MannoseP_isomer; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR01479; GMP_PMI; 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