NODC_RHILO
ID NODC_RHILO Reviewed; 424 AA.
AC P17862; Q52841;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=N-acetylglucosaminyltransferase;
DE EC=2.4.1.-;
DE AltName: Full=Nodulation protein C;
GN Name=nodC; OrderedLocusNames=mlr6163;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NZP 2037;
RX PubMed=2251130; DOI=10.1093/nar/18.22.6690;
RA Collins-Emerson J.M., Terzaghi E.A., Scott D.B.;
RT "Nucleotide sequence of Rhizobium loti nodC.";
RL Nucleic Acids Res. 18:6690-6690(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
RC STRAIN=NZP 2213;
RX PubMed=8850088; DOI=10.1094/mpmi-9-0187;
RA Scott D.B., Young C.A., Collins-Emerson J.M., Terzaghi E.A., Rockman E.S.,
RA Lewis P.E., Pankhurst C.E.;
RT "Novel and complex chromosomal arrangement of Rhizobium loti nodulation
RT genes.";
RL Mol. Plant Microbe Interact. 9:187-197(1996).
CC -!- FUNCTION: Involved in the synthesis of Nod factor, a sulfated N-acyl-
CC beta-1,4-tetrasaccharide of N-acetylglucosamine which initiates a
CC series of events in the host plant species leading eventually to
CC nodulation.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NodC/HAS family. {ECO:0000305}.
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DR EMBL; X52958; CAA37131.1; -; Genomic_DNA.
DR EMBL; BA000012; BAB52500.1; -; Genomic_DNA.
DR EMBL; L06241; AAB47353.1; -; Genomic_DNA.
DR PIR; S12793; S12793.
DR RefSeq; WP_010913821.1; NC_002678.2.
DR AlphaFoldDB; P17862; -.
DR SMR; P17862; -.
DR STRING; 266835.14025901; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PRIDE; P17862; -.
DR EnsemblBacteria; BAB52500; BAB52500; BAB52500.
DR KEGG; mlo:mlr6163; -.
DR eggNOG; COG1215; Bacteria.
DR HOGENOM; CLU_029695_4_2_5; -.
DR OMA; DVIVPCF; -.
DR OrthoDB; 724641at2; -.
DR Proteomes; UP000000552; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR026463; Chitooligosach_Synthase_NodC.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR04242; nodulat_NodC; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycosyltransferase; Membrane; Nodulation; Transferase.
FT CHAIN 1..424
FT /note="N-acetylglucosaminyltransferase"
FT /id="PRO_0000197188"
FT CONFLICT 2
FT /note="N -> T (in Ref. 3; AAB47353)"
FT /evidence="ECO:0000305"
FT CONFLICT 6
FT /note="S -> T (in Ref. 1; CAA37131 and 3; AAB47353)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="P -> A (in Ref. 1; CAA37131)"
FT /evidence="ECO:0000305"
FT CONFLICT 43..44
FT /note="PS -> AG (in Ref. 1; CAA37131)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="C -> S (in Ref. 1; CAA37131)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="D -> E (in Ref. 1; CAA37131)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="H -> Q (in Ref. 1; CAA37131)"
FT /evidence="ECO:0000305"
FT CONFLICT 104..105
FT /note="AG -> GH (in Ref. 1; CAA37131)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="V -> I (in Ref. 1; CAA37131)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="I -> V (in Ref. 1; CAA37131)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="I -> V (in Ref. 1; CAA37131)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="V -> I (in Ref. 1; CAA37131)"
FT /evidence="ECO:0000305"
FT CONFLICT 220..222
FT /note="VSL -> LSV (in Ref. 1; CAA37131)"
FT /evidence="ECO:0000305"
FT CONFLICT 269..271
FT /note="NSM -> DRI (in Ref. 1; CAA37131)"
FT /evidence="ECO:0000305"
FT CONFLICT 292..296
FT /note="AFQLL -> SLHLS (in Ref. 1; CAA37131)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="I -> L (in Ref. 1; CAA37131)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="I -> V (in Ref. 1; CAA37131)"
FT /evidence="ECO:0000305"
FT CONFLICT 341..342
FT /note="MI -> TL (in Ref. 1; CAA37131)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="F -> S (in Ref. 1; CAA37131)"
FT /evidence="ECO:0000305"
FT CONFLICT 399..412
FT /note="ANVQDTGDALPKPN -> TKVARHRARFQKPT (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 417..419
FT /note="DAA -> EAT (in Ref. 1; CAA37131)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 46303 MW; E7121DADB07DAF0E CRC64;
MNLFASASTV AICSYALLST VYKTAQVFYT LPTNVPPTSG DPPSGEPWPS VDVIIPCYNE
APRTLSDCLA SIASQDYAGK LQVYVVDDGS ANRDALVGVH EEYAGDPRFN FVALPKNVGK
RKAQIAAIRR SCGDLVLNVD SDTILAPDVI TRLALKMQDQ AVGAAMGQLA ASNRSETWLT
RLIDMEYWLA CNEERAAQAR FGAVMCCCGP CAMYRRSALV SLLDQYETQR FRGKPSDFGE
DRHLTILMLK AGFRTEYVPE AVAATVVPNS MGPYLRQQLR WARSTFRDTL LAFQLLRGLN
IYLTLDVIGQ NIGPLLLSLS ILAGLAQFVT TGTVPWTACL MIAAMTIVRC SVAAFRARQL
RFLGFSLHTL INIFLLLPLK AYALCTLSNS DWLSRSSAAN VQDTGDALPK PNLVGSDAAY
SEQQ
