ID A0A0Q9YMM8_9COXI Unreviewed; 486 AA.
AC A0A0Q9YMM8;
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=manC1_1 {ECO:0000313|EMBL:KRG21952.1};
GN ORFNames=HT99x_01146 {ECO:0000313|EMBL:KRG21952.1};
OS Candidatus Berkiella aquae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Berkiella.
OX NCBI_TaxID=295108 {ECO:0000313|EMBL:KRG21952.1, ECO:0000313|Proteomes:UP000051497};
RN [1] {ECO:0000313|EMBL:KRG21952.1, ECO:0000313|Proteomes:UP000051497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HT99 {ECO:0000313|EMBL:KRG21952.1,
RC ECO:0000313|Proteomes:UP000051497};
RA Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.;
RT "Draft Genome Sequences of Two Novel Amoeba-resistant Intranuclear
RT Bacteria, Candidatus Berkiella cookevillensis and Candidatus Berkiella
RT aquae.";
RL Submitted (SEP-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 -!- 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:KRG21952.1}.
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DR EMBL; LKAJ01000003; KRG21952.1; -; Genomic_DNA.
DR RefSeq; WP_075065767.1; NZ_LKAJ02000001.1.
DR AlphaFoldDB; A0A0Q9YMM8; -.
DR STRING; 295108.HT99x_01146; -.
DR PATRIC; fig|1590043.3.peg.1158; -.
DR OrthoDB; 9806359at2; -.
DR UniPathway; UPA00126; UER00930.
DR Proteomes; UP000051497; 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: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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:KRG21952.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051497};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRG21952.1}.
FT DOMAIN 4..288
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 316..466
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
FT REGION 467..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 486 AA; 53848 MW; 481520D2A307C216 CRC64;
MLIPVILAGG SGTRLWPLSR ESHPKQFISL FDGQSLFQNT LARVAEIPGC GTPIVMGSEQ
HRFLIAEQVR QSKRPDCAIL LEPMFKGTAP AVALAAMHAL NECDEDVLLL VLPSDHVISD
IKGFLATVSE GVKVAQRGKL VTFGIEPTHP ETGYGYIQKG EALAGSTGFK IGQFVEKPNL
STAKTYIESQ QYWWNSGMFL FSAGAFVQEL MLHHPAIFDA AKAAYCDARF SEDFIRPSSN
EFDKSPADSI DYAVMEKTIN GAMIPLQSAW NDVGAWDALA ELIAKDQQGN AIQGDVITSH
TQNSLIQANH RLVVTVGVDN LVVVETPDAV LILDKSKAQE IKPIVNQMRD NARKEVIFHR
CVNRPWGAFE SIDDGERFQV KRITVAVSQK LSLQRHHHRS EHWVVVKGTA RVTRGEEVFL
LSENQSTYIP IGVNHRLENV GKIPLEIIEV QSGAYLGEDD IVRLDDQYGR SPEKNNEHKA
TTEVEF
//
