ID Q0BV98_GRABC Unreviewed; 495 AA.
AC Q0BV98;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN OrderedLocusNames=GbCGDNIH1_0356 {ECO:0000313|EMBL:ABI61254.1};
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165 {ECO:0000313|EMBL:ABI61254.1, ECO:0000313|Proteomes:UP000001963};
RN [1] {ECO:0000313|EMBL:ABI61254.1, ECO:0000313|Proteomes:UP000001963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1 {ECO:0000313|Proteomes:UP000001963};
RX PubMed=17827295; DOI=10.1128/JB.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J.III., Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(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; CP000394; ABI61254.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0BV98; -.
DR STRING; 391165.GbCGDNIH1_0356; -.
DR KEGG; gbe:GbCGDNIH1_0356; -.
DR eggNOG; COG0662; Bacteria.
DR eggNOG; COG0836; Bacteria.
DR HOGENOM; CLU_035527_1_0_5; -.
DR Proteomes; UP000001963; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Isomerase {ECO:0000313|EMBL:ABI61254.1};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:ABI61254.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001963};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABI61254.1}.
FT DOMAIN 29..310
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 340..490
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 54197 MW; FEBD1C37085881E5 CRC64;
MVPMDQTESG PDSPKAPFQP LSPQEAIIPV ILSGGTGTRL WPVSRESFPK QYWNLTGENS
LIQDTMHRAQ GPQFAPPILV CNQDHRFLIA EQARSAGVEN VRIVLEPCGR NSAPAILAAA
LLAAETNPDS VLWMLAADHS VTRPDALLAA LGKAVAAAKA GYFVTFGMQP TAPETGYGYI
EVGDSITELS GVHRLRRFLE KPDTTTAQAL VSSGQHLWNS GMFVFTARTL IEEMRQHAPA
VLEAVTAAVA GRTQDLDFLR LAREPFVTCP DISLDYAVAE KTSRAAVVPA DIGWSDVGSW
SALWELGDKD DHGNVVQGDA MLESASNCYV RSDGIVTAVI GLKDAVIVTT KDAVLAMHRD
HAQDVKKIVD RLKRSGKPEA ASHNRIYRPW GFYESLIQSD RFQVKRIVVS PGHRLSLQKH
YHRAEHWVVV AGTAIVTRDE EDILVRENES IYLPLGTVHR LSNPGHIPLA LIEVQSGAYL
GEDDIVRLED TYGRQ
//
