ID   XANB_XANCP              Reviewed;         467 AA.
AC   P0C7J3; P29956; Q93S98;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Xanthan biosynthesis protein XanB;
DE   Includes:
DE     RecName: Full=Mannose-6-phosphate isomerase;
DE              EC=5.3.1.8;
DE     AltName: Full=Phosphohexomutase;
DE     AltName: Full=Phosphomannose isomerase;
DE              Short=PMI;
DE   Includes:
DE     RecName: Full=Mannose-1-phosphate guanylyl transferase;
DE              EC=2.7.7.13;
DE     AltName: Full=GDP-mannose pyrophosphorylase;
DE              Short=GMP;
DE              Short=GMPP;
GN   Name=xanB; OrderedLocusNames=XCC0625;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
CC   -!- FUNCTION: Involved in xanthan production. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannose 6-phosphate = D-fructose 6-phosphate;
CC         Xref=Rhea:RHEA:12356, ChEBI:CHEBI:58735, ChEBI:CHEBI:61527;
CC         EC=5.3.1.8;
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   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC       biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP
CC       route): step 1/1.
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC       biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC       step 1/2.
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; AE008922; AAM39941.1; -; Genomic_DNA.
DR   RefSeq; NP_636017.1; NC_003902.1.
DR   RefSeq; WP_011035868.1; NC_003902.1.
DR   AlphaFoldDB; P0C7J3; -.
DR   SMR; P0C7J3; -.
DR   STRING; 340.xcc-b100_3730; -.
DR   EnsemblBacteria; AAM39941; AAM39941; XCC0625.
DR   KEGG; xcc:XCC0625; -.
DR   PATRIC; fig|190485.4.peg.686; -.
DR   eggNOG; COG0662; Bacteria.
DR   eggNOG; COG0836; Bacteria.
DR   HOGENOM; CLU_035527_1_0_6; -.
DR   OMA; QRPMYEE; -.
DR   UniPathway; UPA00126; UER00423.
DR   UniPathway; UPA00126; UER00930.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase activity; IBA:GO_Central.
DR   GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
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   Exopolysaccharide synthesis; GTP-binding; Isomerase;
KW   Lipopolysaccharide biosynthesis; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..467
FT                   /note="Xanthan biosynthesis protein XanB"
FT                   /id="PRO_0000194252"
SQ   SEQUENCE   467 AA;  50962 MW;  77C8B346D7F25E3B CRC64;
     MSDVLPIILS GGSGTRLWPL SRESYPKQFL PLVGEHSMLQ ATWLRSAPVA AHAPIVVANE
     EHRFMAAEQL QQLGVKPSAI LLEPKGRNTA PAIAVAALEA TRNGGDPLLL VLPSDHVIRD
     EAAFQAAVTV AAAAAEQGKL VTFGIKPTAP ETGYGYIKAG VGTGATAVER FVEKPDLATA
     QGYLASGEYY WNSGMFLFRA SRYLEELRKF QPAIADACQK AWEGGKRDAD FTRLDKDAFA
     SSPSDSIDYA VMEKTADAVV VPLDAGWNDV GSWSSLLDVS EQDGQGNAHH GDVIQLDCKN
     TYAYGSRLIA MVGLENVVVV ETDDAVLVGH RDRIQEVKEV VSQIKSAGRS EATWHRKVYR
     PWGAYDSIDM GQRFQVKRIT VKPGATLSLQ MHHHRAEHWI VVSGTAEVTR GEEVLLLTEN
     QSTYIPLGVT HRLKNPGKLP LELIEVQSGS YLGEDDIVRF EDTYGRT