ID A0A0Q6Z3Z4_9BRAD Unreviewed; 470 AA.
AC A0A0Q6Z3Z4;
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:KQW22323.1};
GN ORFNames=ASC80_02710 {ECO:0000313|EMBL:KQW22323.1};
OS Afipia sp. Root123D2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1736436 {ECO:0000313|EMBL:KQW22323.1, ECO:0000313|Proteomes:UP000051348};
RN [1] {ECO:0000313|EMBL:KQW22323.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW22323.1,
RC ECO:0000313|Proteomes:UP000051348};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW22323.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW22323.1,
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:KQW22323.1}.
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DR EMBL; LMDP01000001; KQW22323.1; -; Genomic_DNA.
DR RefSeq; WP_056292641.1; NZ_LMDP01000001.1.
DR AlphaFoldDB; A0A0Q6Z3Z4; -.
DR STRING; 1736436.ASC80_02710; -.
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:KQW22323.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051348};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KQW22323.1}.
FT DOMAIN 7..286
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 316..465
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
SQ SEQUENCE 470 AA; 51194 MW; 0BC17CB2DCEB58B5 CRC64;
MSERIIPLIM CGGAGTRLWP ASREGRPKQF LQLFGSRSTF QETLLRVSDA TLFERPVIIT
NNAYRFMVLE QLAAVEIEAD VLLEPVRRDS GPAIAAGAAF ALTRSADAVV LALAADHVVR
DTAAFAEACR KALSVASAGR IVTFGVQPER PATEYGYIRP GEEIFGGVSA VAAFVEKPDA
VTAAGYVKDG YLWNSGNFMF RAQMLLDEYA RMDAGSVQAV RDAVKEAGRD LGFVLLDPEA
FGKAKAISID YAVMEKTKQA AVVPVSCGWS DVGSWHAVWE LSDKDDHGNA AQGTAVFEGA
TNCNVSTDKA LVALEGVDDL VVVATQDAVL VSRQKDPAGL KRLVAKLKKV APEVTADHLK
VHRPWGSYQS LDIGDRHQVK RIIVKAGGRL SLQKHHHRSE HWIVVRGAAL VTVNETEKIV
HENESIYIPI GATHRMENPG KIPLELIEVQ TGSYLGEDDI IRIEDDYRRS
//
