ID A0A0Q6Z3K0_9BRAD Unreviewed; 475 AA.
AC A0A0Q6Z3K0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN Name=cpsB {ECO:0000313|EMBL:KQW18340.1};
GN ORFNames=ASC80_20095 {ECO:0000313|EMBL:KQW18340.1};
OS Afipia sp. Root123D2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1736436 {ECO:0000313|EMBL:KQW18340.1, ECO:0000313|Proteomes:UP000051348};
RN [1] {ECO:0000313|EMBL:KQW18340.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW18340.1,
RC ECO:0000313|Proteomes:UP000051348};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW18340.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW18340.1,
RC ECO:0000313|Proteomes:UP000051348};
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:KQW18340.1}.
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DR EMBL; LMDP01000004; KQW18340.1; -; Genomic_DNA.
DR RefSeq; WP_056301316.1; NZ_LMDP01000004.1.
DR AlphaFoldDB; A0A0Q6Z3K0; -.
DR STRING; 1736436.ASC80_20095; -.
DR OrthoDB; 9806359at2; -.
DR Proteomes; UP000051348; 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:KQW18340.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051348};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KQW18340.1}.
FT DOMAIN 8..291
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 320..470
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
SQ SEQUENCE 475 AA; 51383 MW; 1345609418FDCFE7 CRC64;
MPHGRITPVL LSGGSGSRLW PLSRETYPKQ LLSLLGEKTM LQQTALRVGD PAVFGDPIVV
ANTEHRFAIA EQLRAVGVDQ PAMVLEPFGR NTAPAVAIAA LIASEADPDA IILVMPVDHW
VRDAAAFGAA MVAGLAAARQ GKFVLFGVRP TSPATGFGYI RVGDKLPAAS GIHAVAGFTE
KPTLQTAEKF LAAKDHLWNS GIFLLPARQF IEELSRLAPE VLAASRAALA DAARDLDFLR
LDEAAFKNCP AISIDHAVME KTASAAVLPV AFDWSDVGSW SALWKMADKD DDGNVAIGDV
VMEDATGCYV RGEGPLVAAI GVEDLIITAT PDVVLVSTKD RDQDVSKVVS KLKANGHRSA
TQTQCVHRPW GYYQSIHAGD RFQVKRITVN PGAKLSLQKH FHRAEHWVVV NGTAIVTRDD
EEILLRENES VFVPLGCMHR LENPGKVPLN LIEVQSGPYL GEDDIVRIED VYHRI
//
