ID A0A063Y482_9GAMM Unreviewed; 471 AA.
AC A0A063Y482;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN ORFNames=ADINL_0216 {ECO:0000313|EMBL:KDE41143.1};
OS Nitrincola lacisaponensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Nitrincola.
OX NCBI_TaxID=267850 {ECO:0000313|EMBL:KDE41143.1, ECO:0000313|Proteomes:UP000027318};
RN [1] {ECO:0000313|EMBL:KDE41143.1, ECO:0000313|Proteomes:UP000027318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4CA {ECO:0000313|EMBL:KDE41143.1,
RC ECO:0000313|Proteomes:UP000027318};
RX PubMed=16280482; DOI=10.1099/ijs.0.63647-0;
RA Dimitriu P.A., Shukla S.K., Conradt J., Marquez M.C., Ventosa A.,
RA Maglia A., Peyton B.M., Pinkart H.C., Mormile M.R.;
RT "Nitrincola lacisaponensis gen. nov., sp. nov., a novel alkaliphilic
RT bacterium isolated from an alkaline, saline lake.";
RL Int. J. Syst. Evol. Microbiol. 55:2273-2278(2005).
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:KDE41143.1}.
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DR EMBL; JMSZ01000007; KDE41143.1; -; Genomic_DNA.
DR RefSeq; WP_036542817.1; NZ_JMSZ01000007.1.
DR AlphaFoldDB; A0A063Y482; -.
DR STRING; 267850.ADINL_0216; -.
DR PATRIC; fig|267850.7.peg.212; -.
DR OrthoDB; 9806359at2; -.
DR UniPathway; UPA00126; UER00930.
DR Proteomes; UP000027318; 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:KDE41143.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027318};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KDE41143.1}.
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"
SQ SEQUENCE 471 AA; 52625 MW; 13BEBAC83C7EAED3 CRC64;
MLLPVIIAGG TGSRLWPLSR QLKPKQFLKL CGDATLLQQT LRRLDGLEAT SPAIICNEDH
RFMVAEQLRQ LEVKDAIILL EPMGRNTAPA IALAALNAIQ TSRDPILLVL AADHFIADQC
AFQKVVLEAK KLAEQDKLVT FGIVPTQPET GFGYIQRGDD LPITGYKVAR FVEKPDLMRA
QEYLESGDYY WNSGMFMFKA SVYLKALAKF RPDILKACKK SLQQGQQGQQ SMDFVRVDAE
AFAQCPEDSI DYAVMEKTDD AAVIPLDAGW SDIGSWSALW DIGKKDAQGN VCEGDVLLLN
SENSFVYADS RLITTLGIDN LMVIETKDAV LVAHKDQVQD VKKIVEMLKQ SGRKEYISHR
QVYRPWGVYD SIENGERYQV KRITVKPGAK LSVQMHHHRA EHWIVVSGTA KVTKGGKTFL
MTENESTYIS IGEVHALENP GTIPLELIEV QSGSYLGEDD IVRFEDQYGR V
//
