ID A0A149Q4H5_9PROT Unreviewed; 479 AA.
AC A0A149Q4H5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:KXU92230.1};
GN ORFNames=AD928_11990 {ECO:0000313|EMBL:KXU92230.1};
OS Acetobacter cerevisiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=178900 {ECO:0000313|EMBL:KXU92230.1, ECO:0000313|Proteomes:UP000075473};
RN [1] {ECO:0000313|EMBL:KXU92230.1, ECO:0000313|Proteomes:UP000075473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 1625 {ECO:0000313|EMBL:KXU92230.1,
RC ECO:0000313|Proteomes:UP000075473};
RA Li L., Cleenwerck I., De Vuyst L., Vandamme P.;
RT "Improved classification and identification of acetic acid bacteria using
RT matrix-assisted laser desorption/ionization time-of-flight mass
RT spectrometry; Gluconobacter nephelii and Gluconobacter uchimurae are later
RT heterotypic synonyms of Gluconobacter japonicus and Gluconobacter oxydans,
RT respectively.";
RL Submitted (JUN-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:KXU92230.1}.
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DR EMBL; LHZA01000155; KXU92230.1; -; Genomic_DNA.
DR RefSeq; WP_062250816.1; NZ_LHZA01000155.1.
DR AlphaFoldDB; A0A149Q4H5; -.
DR PATRIC; fig|178900.5.peg.840; -.
DR Proteomes; UP000075473; 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:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:KXU92230.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075473};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KXU92230.1}.
FT DOMAIN 13..295
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 325..474
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
SQ SEQUENCE 479 AA; 52772 MW; 48DE412C817D2057 CRC64;
MTSRPAGSKM IVPVVLSGGT GSRLWPMSRA SFPKQLWSLV SERSMLQETV LRGNAAGFAP
PVIVCNEEHR FLIAEQLREV SVANPSIMLE PVGRNSAPAI TAAALLVAQT HPDAVLWMMA
ADADIKKSDA LTQAMEKAVQ AAEQGRVVTF GMTPTCPETG YGYIEKGDPL PGVDGAFTIR
SFREKPLQAV AEDFVKDGNY FWNSGMFVFR ADVLLAEMHR YAPQVLQSVQ EAFEKRKTDL
DFIRLDKEAF AQAPDISIDY AVAEHTQVSA VIPADLGWSD VGSWDALWEI SPKTAEGNVL
LGDVLAEDAH GCYVRSEGPL TAVTGLDDVV VVVTGDAVLV THKDRAQDVK KVVDRLKKDG
RPEASTHQRN YRPWGFYEGL TRNERFQVKR IVVNPGGKLS LQKHFHRAEH WVVVEGVALV
TKGDAELLVR ENESVYLPQG CVHRLENPGK IPLTLIEVQS GAYLGEDDII RLEDSYNRN
//
