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Database: UniProt
Entry: A0A0M2S5K2_9ACTN
LinkDB: A0A0M2S5K2_9ACTN
Original site: A0A0M2S5K2_9ACTN 
ID   A0A0M2S5K2_9ACTN        Unreviewed;       630 AA.
AC   A0A0M2S5K2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase {ECO:0000256|ARBA:ARBA00012519};
DE            EC=2.7.7.70 {ECO:0000256|ARBA:ARBA00012519};
GN   ORFNames=LQ51_03490 {ECO:0000313|EMBL:KKK07274.1};
OS   Micromonospora sp. HK10.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1538294 {ECO:0000313|EMBL:KKK07274.1, ECO:0000313|Proteomes:UP000034330};
RN   [1] {ECO:0000313|EMBL:KKK07274.1, ECO:0000313|Proteomes:UP000034330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HK10 {ECO:0000313|EMBL:KKK07274.1,
RC   ECO:0000313|Proteomes:UP000034330};
RA   Talukdar M., Das D., Borah C., Deka Boruah H.P., Bora T.C., Singh A.K.;
RT   "Draft genome sequence of Micromonospora HK10, isolated from Kaziranga
RT   National park, Assam, India.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glycero-beta-D-manno-heptose 1-phosphate + H(+) = ADP-
CC         D-glycero-beta-D-manno-heptose + diphosphate; Xref=Rhea:RHEA:27465,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:59967, ChEBI:CHEBI:61593; EC=2.7.7.70;
CC         Evidence={ECO:0000256|ARBA:ARBA00000534};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004713}.
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:KKK07274.1}.
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DR   EMBL; JTGL01000024; KKK07274.1; -; Genomic_DNA.
DR   RefSeq; WP_046566376.1; NZ_KQ058826.1.
DR   AlphaFoldDB; A0A0M2S5K2; -.
DR   STRING; 1538294.LQ51_03490; -.
DR   PATRIC; fig|1538294.3.peg.3252; -.
DR   HOGENOM; CLU_021150_2_1_11; -.
DR   OrthoDB; 9802794at2; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000034330; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1190.20; -; 2.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR011611; PfkB_dom.
DR   InterPro; IPR011914; RfaE_dom_II.
DR   InterPro; IPR029056; Ribokinase-like.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR   NCBIfam; TIGR02199; rfaE_dom_II; 1.
DR   PANTHER; PTHR43793:SF2; BIFUNCTIONAL PROTEIN HLDE; 1.
DR   PANTHER; PTHR43793; FAD SYNTHASE; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   Pfam; PF00294; PfkB; 2.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
DR   PROSITE; PS00583; PFKB_KINASES_1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          23..123
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
FT   DOMAIN          364..445
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
FT   DOMAIN          488..583
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
FT   REGION          235..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..255
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   630 AA;  64898 MW;  45AEB26F95F84495 CRC64;
     MAGAAAEERR LATVVESWLG RPVLVVGDAM LDEWRFAESD RLCREAPAPV LTLRRRISAA
     GGAANTAVNV AALGGRAALV APVGADVAGD ELHDCLDRAG VWDRTVNQPG RPTPVKRRML
     AGNQILLRED SGDPDDALDD DGVARLLTAL HCATEELHAA AHGQPLTLVV CDYGLGALPG
     GVRAWLVANR DRYATVALDA HDLADWRGLN PTVVTPSFAE ATRLLARAAA GFNGAGHPPR
     RVDGLHLDHQ DDPADGPSEL VVGAAPGGAG EPAPVPDPLR DGSSLAMGSA PAGHRPPGTP
     HPTSGTAPAA AGPTGEPTPG EERVALTGDG LSVTGTGVTV NAEVGEGVDR AVLAQSRLDE
     LRAHTGADVV AVTLDTEGAV VGGADGEPRR SHSTPVPASH AVGAGDAYLA AMTLALAAEA
     SLPTAAQLAQ LAATITVSDT GTCVCRREDL LDALGTGPEE GDHPTLVGAA ELGAIVTEHR
     RAGRSIVFTN GCFDVLHPGH VRYLTQARAL GDLLVVAVNS DGSVRRLKGP DRPVNPVEDR
     AALLAALECV DHVVVFEEDS PAGLIEAVRP DVYVKGGDYP PEMVPEAPLV RRLGGQVRTL
     GYVPDRSTSA IIDRIRAQSV TPPVGEGRSA
//
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