ID A0A0C1J007_9RHOB Unreviewed; 472 AA.
AC A0A0C1J007;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN Name=cpsB {ECO:0000313|EMBL:KIC41332.1};
GN ORFNames=RA27_10680 {ECO:0000313|EMBL:KIC41332.1};
OS Ruegeria sp. ANG-R.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1577903 {ECO:0000313|EMBL:KIC41332.1, ECO:0000313|Proteomes:UP000031318};
RN [1] {ECO:0000313|Proteomes:UP000031318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-R {ECO:0000313|Proteomes:UP000031318};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIC41332.1}.
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DR EMBL; JWLJ01000003; KIC41332.1; -; Genomic_DNA.
DR RefSeq; WP_039539015.1; NZ_JWLJ01000003.1.
DR AlphaFoldDB; A0A0C1J007; -.
DR STRING; 1577903.RA27_10680; -.
DR OrthoDB; 9806359at2; -.
DR Proteomes; UP000031318; Unassembled WGS sequence.
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:KIC41332.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KIC41332.1}.
FT DOMAIN 4..277
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 314..464
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
SQ SEQUENCE 472 AA; 51741 MW; E083CD5B909E9606 CRC64;
MIQPIILAGG SGTRLWPVSR KSYPKQFVEL DGDNSLFQKT VERVAEPGFS APLIVTGEDY
RFIAQQQLAD VDAEKSELIV EPVGRNTAAA VLAAALRYKE EPETILLVLP SDHAIEDVSA
FRRTMVRAEK TAKRGKIVTF GIKPDHAATG FGYLRVAGGY QGALLISTFA EKPDAQTAKV
MLESGDWLWN AGMFMFRVDT VLKAFEAHAP EMSAPVEAAV ALGQKDLGFY RLDQNAFFRC
PSLSFDHAVM EHVEKGVVAF ELDCGWSDLG SWKSVKDQGQ LDEGANVTSG NSTAIDCRDS
LLRSENPDIK LVGLGLKDIV AVATDDGILV ADMSHSAEVG KVVDALRNEG SDQAEMFRRC
HRPWGYYETL SLGSRFQVKR IMVLPGAKLS LQSHMHRAEH WVVVSGSATV TVGDRVSLLS
ENESTYIPLG AVHRLENPGK LPLHLIEVQS GCYLGEDDIV RYEDIYDRVA VA
//