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Database: UniProt
Entry: A0A0Q5DQY6_9BURK
LinkDB: A0A0Q5DQY6_9BURK
Original site: A0A0Q5DQY6_9BURK 
ID   A0A0Q5DQY6_9BURK        Unreviewed;       472 AA.
AC   A0A0Q5DQY6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   ORFNames=ASF61_18205 {ECO:0000313|EMBL:KQQ46335.1};
OS   Duganella sp. Leaf126.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ46335.1, ECO:0000313|Proteomes:UP000051032};
RN   [1] {ECO:0000313|EMBL:KQQ46335.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ46335.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ46335.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ46335.1};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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}.
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:KQQ46335.1}.
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DR   EMBL; LMNW01000002; KQQ46335.1; -; Genomic_DNA.
DR   RefSeq; WP_056151329.1; NZ_LMNW01000002.1.
DR   AlphaFoldDB; A0A0Q5DQY6; -.
DR   STRING; 1736266.ASF61_18205; -.
DR   OrthoDB; 9806359at2; -.
DR   Proteomes; UP000051032; Unassembled WGS sequence.
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; 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:ARBA00023134};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:KQQ46335.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KQQ46335.1}.
FT   DOMAIN          5..287
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          317..467
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   472 AA;  52112 MW;  E06340B7438D4B68 CRC64;
     MKIYPVILSG GAGTRLWPLS RAMMPKQLLP LVSQRSMLQE TVMRLPEGET MAAPLIVCGS
     DHRFMVAEQM REIGIASLGI LLESTGRNTA PAVAAAAHFL LAQDPDAVML VLPADHVIED
     RAGFHGAIAR AAELAENGAL ATFGILPTSP ETGYGYIRRG TPVAAESGSY RVERFVEKPD
     LATAQGFLAD GGYYWNSGMF VFQARTYVDE LRALQPAMEA SAAEAVRLAY RDLDFCRLDE
     AAFAASPSES IDYAVMEHTR RAVVVAADIG WNDVGSWSAL WEVQQRDVEG NTTRGDVYLD
     GVTNSLVRAE SRIVAVIGVR DLVVVETADA VLVTHRDRVQ RVKKVVERLH ADHRTEHLHH
     RRVYRPWGSY EGIDVGDRFQ VKRIVVNPGG KLSLQMHHHR AEHWIVVSGT ARVTCGDTVT
     LLSENQSTYI PIGMNHRLEN PGKLPLHLIE VQSGSYLGED DIVRFEDVYQ RA
//
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