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Database: UniProt
Entry: A0A1X6ZKL0_9RHOB
LinkDB: A0A1X6ZKL0_9RHOB
Original site: A0A1X6ZKL0_9RHOB 
ID   A0A1X6ZKL0_9RHOB        Unreviewed;       481 AA.
AC   A0A1X6ZKL0;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   Name=algA {ECO:0000313|EMBL:SLN53675.1};
GN   ORFNames=ROJ8625_02744 {ECO:0000313|EMBL:SLN53675.1};
OS   Roseivivax jejudonensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseivivax.
OX   NCBI_TaxID=1529041 {ECO:0000313|EMBL:SLN53675.1, ECO:0000313|Proteomes:UP000193570};
RN   [1] {ECO:0000313|EMBL:SLN53675.1, ECO:0000313|Proteomes:UP000193570}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8625 {ECO:0000313|EMBL:SLN53675.1,
RC   ECO:0000313|Proteomes:UP000193570};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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; FWFK01000004; SLN53675.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X6ZKL0; -.
DR   OrthoDB; 9806359at2; -.
DR   Proteomes; UP000193570; 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   Reference proteome {ECO:0000313|Proteomes:UP000193570};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..289
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          321..471
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   481 AA;  52110 MW;  DB5609EEF35F66BD CRC64;
     MHKIHPVILC GGSGTRLWPL SRKSYPKQFT PMMGDETLFQ GTALRLSGAT DGIAFEKPVI
     VTNSDFRFVV TEQLSRVGID PGAILIEPAG RNTAPAVLAA ALHLEARDPD AIMLVAPSDH
     LIRDAAGFHA AIARGLPSVD AGHLTLFGIT PDRPETGYGY LQLAEAANGG PVPLHSFVEK
     PDAETAARML SDGSYLWNAG IFLFRARDIV AAFERLAAEV VPPVGAALRQ AEVDLGFLRL
     DPEAWDAAPD ISIDYAVMEK AEDLHVVPYD GDWSDLGGWD AVWRASEMDD DGNAAGEGAT
     AIDCRNTLLR SDSERLELVG IGLDDMIAVA MKDAVLVAPK SRAQDVKKAV SALREKEAAQ
     AETFPLDHRP WGWFESLVVG SRFQVKRILV HPGASLSLQS HFHRSEHWIV VEGTARVTVD
     DEVTLVTENE SVYIPLGAVH RMENPGKVPM VLIEVQTGSY VGEDDIVRYE DVYARGQGAK
     G
//
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