ID A0A1V3PW21_9GAMM Unreviewed; 470 AA.
AC A0A1V3PW21;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN ORFNames=B0E47_13350 {ECO:0000313|EMBL:OOG54146.1};
OS Rhodanobacter sp. B05.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1945859 {ECO:0000313|EMBL:OOG54146.1, ECO:0000313|Proteomes:UP000188464};
RN [1] {ECO:0000313|EMBL:OOG54146.1, ECO:0000313|Proteomes:UP000188464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05 {ECO:0000313|EMBL:OOG54146.1,
RC ECO:0000313|Proteomes:UP000188464};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-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 -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00004823}.
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:OOG54146.1}.
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DR EMBL; MUNU01000017; OOG54146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3PW21; -.
DR STRING; 1945859.B0E47_13350; -.
DR OrthoDB; 9806359at2; -.
DR UniPathway; UPA00126; UER00930.
DR Proteomes; UP000188464; 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:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
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:OOG54146.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:OOG54146.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000188464};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OOG54146.1}.
FT DOMAIN 4..278
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 315..465
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
SQ SEQUENCE 470 AA; 51664 MW; 49988D3D2AB712D0 CRC64;
MLIPLILSGG SGTRLWPVSR KNLPKQFLAL AGRGTLFQQT VARTRQLPEV AAPIVVASED
HRFLAADQLL EAGIEGATIV LEPLARNTAP AIALGALQAL QRDPEAILLV LPADHLIGDQ
AAFVEAVQQA WPLAEKGWLV TFGVRPDRAE TGFGYIRHAE AIDNHGFRVG QFVEKPDQAT
AESYLADGSY DWNSGMFLFQ ASRYLEELAA HAPVMLAAVR EAHAKASTDL DFVRVDRDAF
ARVPDDSIDY AVMEKTQRAA VIPVSCAWSD IGSWSALWLS GGKDADGNLR EGDTMPVDTR
NSLLRSHDRH LLATVGVDDL IVVTTPDATL VAHRDAAQDV KKIVEQLKAA GRSEHSLHRM
VYRPWGNYDS LEEGERFQVK RIVVKPGASL SLQKHHHRAE HWIVVSGTAE VTCDDKVFLL
GENQSTYIPL GSKHRLRNPG KVALELIEVQ SGSYLGEDDI VRYDDVYGRV
//
