GenomeNet

Database: UniProt
Entry: D5SVV2_PLAL2
LinkDB: D5SVV2_PLAL2
Original site: D5SVV2_PLAL2 
ID   D5SVV2_PLAL2            Unreviewed;       321 AA.
AC   D5SVV2;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000313|EMBL:ADG69462.1};
GN   OrderedLocusNames=Plim_3650 {ECO:0000313|EMBL:ADG69462.1};
OS   Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290)
OS   (Planctomyces limnophilus).
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Planctopirus.
OX   NCBI_TaxID=521674 {ECO:0000313|EMBL:ADG69462.1, ECO:0000313|Proteomes:UP000002220};
RN   [1] {ECO:0000313|EMBL:ADG69462.1, ECO:0000313|Proteomes:UP000002220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / 290
RC   {ECO:0000313|Proteomes:UP000002220};
RX   PubMed=21304691; DOI=10.4056/sigs.1052813;
RA   Labutti K., Sikorski J., Schneider S., Nolan M., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Tindall B.J., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Planctomyces limnophilus type strain (Mu
RT   290).";
RL   Stand. Genomic Sci. 3:47-56(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP =
CC         diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23;
CC         Evidence={ECO:0000256|ARBA:ARBA00001851};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-
CC         acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157;
CC         Evidence={ECO:0000256|ARBA:ARBA00000731};
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC       hexapeptide repeat family. {ECO:0000256|ARBA:ARBA00007707}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC       acetylglucosamine-1-phosphate uridyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00007947}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001744; ADG69462.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5SVV2; -.
DR   STRING; 521674.Plim_3650; -.
DR   KEGG; plm:Plim_3650; -.
DR   eggNOG; COG1207; Bacteria.
DR   HOGENOM; CLU_029499_15_0_0; -.
DR   OrthoDB; 9775031at2; -.
DR   Proteomes; UP000002220; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02540; GT2_GlmU_N_bac; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR025877; MobA-like_NTP_Trfase.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   PANTHER; PTHR43584:SF3; BIFUNCTIONAL PROTEIN GLMU; 1.
DR   PANTHER; PTHR43584; NUCLEOTIDYL TRANSFERASE; 1.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF12804; NTP_transf_3; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002220};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADG69462.1}.
FT   DOMAIN          6..136
FT                   /note="MobA-like NTP transferase"
FT                   /evidence="ECO:0000259|Pfam:PF12804"
SQ   SEQUENCE   321 AA;  34285 MW;  50C2B1071A36FC42 CRC64;
     MAAPLAIVLA AGKSTRMKSA LPKVVHPLFG RPMVEYVFDA ARAAGVERLV VVVGHRADEV
     QAILAHHKDV EFALQTEQKG TGHAVKMCLP ALQTHQGPVL ILSGDTPLLK VDSLKKLLAA
     QGAGAAAVIG TAKTQANEGL GRIVRSPEGE FLRIVEERDA TPAEKRIQEI NTGCYAFDGQ
     KLASALERLQ PTNAQGEYYL TDAPALLKAD RELVIAADCF DIEEAMGVNT RIQLAEVAQV
     IKDRTDRQLM AEGVTIVDPR LVSIDPQAKI AADVVIEPFV VIRGAVEIGP DSHIGPHAVL
     EGPLTLPGGS IVKPFQHLPS R
//
DBGET integrated database retrieval system