ID A0A0D6MSC4_ACEAC Unreviewed; 441 AA.
AC A0A0D6MSC4; A0A7G1M5G6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, 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=Abac_009_015 {ECO:0000313|EMBL:GAN56602.1};
OS Acetobacter aceti NBRC 14818.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter; Acetobacter subgen. Acetobacter.
OX NCBI_TaxID=887700 {ECO:0000313|EMBL:GAN56602.1, ECO:0000313|Proteomes:UP000032677};
RN [1] {ECO:0000313|EMBL:GAN56602.1, ECO:0000313|Proteomes:UP000032677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 14818 {ECO:0000313|EMBL:GAN56602.1,
RC ECO:0000313|Proteomes:UP000032677};
RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT "Whole genome sequence of Acetobacter aceti NBRC 14818.";
RL Submitted (NOV-2012) 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:GAN56602.1}.
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DR EMBL; BAMU01000009; GAN56602.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D6MSC4; -.
DR Proteomes; UP000032677; 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: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 Isomerase {ECO:0000313|EMBL:GAN56602.1};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:GAN56602.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:GAN56602.1}.
FT DOMAIN 4..257
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 287..436
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
SQ SEQUENCE 441 AA; 48777 MW; 17BA0B9F779DB0D9 CRC64;
MLSAQSLLQE TALRARGISL SAPVIVCNEA HRFLIAEQLR EAGIESPKIL LEPVGRNSAP
AIAAAALLVA QTDPQAVLWL MAADAAITKP EALNTAMQNA IAGAEQGLVV TFGMKPTRPE
TGYGYIEVGQ TISGLEGIST VKAFREKPDE EQAEFFLKSG DYLWNSGMFV FRADTLLREM
EEHAPEVMTA VRAAYEARKG DLFFERLGIE EFKTAPDISI DYAIAERSSN VAVVPADLGW
SDVGSWDALW DISPKDTAGN VAVGDVLIED SKNSYVRSEK YLTAVAGVDD LVVVTTDDAV
LVTHRDRAQD VKKIVDRLKK AKRPEAASHN RCYRPWGFYE SLIQNDRFQV KRIVVQPGEK
LSLQKHFHRA EHWIVVGGVA LVTRDEDKVL VRENESIYLP QGCIHRMENP GKIPLTLIEV
QTGAYLGEDD IVRLEDTYNR S
//
