ID A0A0Q5HJR9_9BURK Unreviewed; 472 AA.
AC A0A0Q5HJR9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN ORFNames=ASF77_09130 {ECO:0000313|EMBL:KQQ88871.1};
OS Massilia sp. Leaf139.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ88871.1, ECO:0000313|Proteomes:UP000051760};
RN [1] {ECO:0000313|EMBL:KQQ88871.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ88871.1,
RC ECO:0000313|Proteomes:UP000051760};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ88871.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ88871.1,
RC ECO:0000313|Proteomes:UP000051760};
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:KQQ88871.1}.
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DR EMBL; LMOJ01000022; KQQ88871.1; -; Genomic_DNA.
DR RefSeq; WP_056339205.1; NZ_LMOJ01000022.1.
DR AlphaFoldDB; A0A0Q5HJR9; -.
DR STRING; 1736272.ASF77_09130; -.
DR OrthoDB; 9806359at2; -.
DR Proteomes; UP000051760; 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:KQQ88871.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051760};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KQQ88871.1}.
FT DOMAIN 5..288
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; 51515 MW; 6332FE9BB3B494B7 CRC64;
MKIYPVILSG GAGTRLWPLS RAVLPKQLLP IVADKTMLQD TALRVAGLPG LQAPLVVCGN
DHRFMVAEQL RAAGITPLGI LLEPVGRNTA PAVAAAAHFL KSIDPEAVML VLPADHVIEN
TEAFKEAVAR AASLVQGGGL ATFGIVPKSP ETGYGYIRRG APLAACDGCY QVERFVEKPD
LATAEGFVAD GGYYWNSGMF MFAAEQYLSE LAQYAPKIAA AAEQAIGTGY RDLDFCRLDE
TAFSNCPSDS IDYAVMEHTA NAVVVPADIG WSDVGSWSAL WEVQPHDEHG NSQRGDVYLD
GVKNSLVRAE SRIVAVVGLE DVVVVETNDA VLVAHKSAVQ RVKQVVDHLK SKERTEHLHH
TKVYRPWGHY EGIDAGDRFQ VKRITVKPGE KLSLQMHHHR AEHWVVVSGT ARVTCGEKIS
LLSENESTYI PIGMNHRLEN PGKLPLHIIE VQSGSYLGED DIVRFEDIYK RS
//