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Database: UniProt
Entry: A0A1H2WXV0_9RHOB
LinkDB: A0A1H2WXV0_9RHOB
Original site: A0A1H2WXV0_9RHOB 
ID   A0A1H2WXV0_9RHOB        Unreviewed;       483 AA.
AC   A0A1H2WXV0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   ORFNames=SAMN05444336_102533 {ECO:0000313|EMBL:SDW85367.1};
OS   Albimonas donghaensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Albimonas.
OX   NCBI_TaxID=356660 {ECO:0000313|EMBL:SDW85367.1, ECO:0000313|Proteomes:UP000199118};
RN   [1] {ECO:0000313|EMBL:SDW85367.1, ECO:0000313|Proteomes:UP000199118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17890 {ECO:0000313|EMBL:SDW85367.1,
RC   ECO:0000313|Proteomes:UP000199118};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNMZ01000002; SDW85367.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2WXV0; -.
DR   STRING; 356660.SAMN05444336_102533; -.
DR   Proteomes; UP000199118; Unassembled WGS sequence.
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: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   Isomerase {ECO:0000313|EMBL:SDW85367.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:SDW85367.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199118};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SDW85367.1}.
FT   DOMAIN          18..292
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          328..478
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   483 AA;  52361 MW;  915516C397580DF0 CRC64;
     MESVFGGVAR KMTRKIYPVI LCGGSGTRLW PLSRKSYPKQ FSALMGEASL FQLTLKRLSG
     EGYADPVLLT NSDFRFIATQ QLGEAGGNAS KILIEPAARN TAPAILAAAV ALADEPDALM
     LVAPSDHVIK DDAAFRLAVD AAAGAAEAGQ LVTFGITPDR PETGYGYLEL ETAPDAGAQP
     LKRFVEKPDA EAAAEMLATG RFLWNAGIFM FKVSTILKAF EDHAPGLMAP VRASVAEGAT
     DLCFFRLGET AYMGAEDISI DYAVMERAAN LTVVPFNGGW NDLGSWETVW RETGPDADGV
     ATTQGATAID CKNTFLRTDS EGTRLVGIGL ENIVAVAMQD AVLVADIRQS QRVKEAVAAL
     KLENAGQAED FPRFHRPWGW YETLSLGRRF QVKRIMVYPG GQLSLQSHVH RSEHWVVVEG
     TAKVTVGEEV KLLSENQSVY IPLGAVHRME NPGKVPMYLI EVQSGPYLGE DDIIRYEDVY
     ARA
//
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