UniProt: D3P581

Database: UniProt
Entry: D3P581_AZOS1

LinkDB:  D3P581_AZOS1 
Original site:  D3P581_AZOS1

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Ontology (6)   
   GO (5)   
   CAZY (1)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (4)   
   Pfam (2)   
Literature (1)   
   PubMed (1)   
All databases (17)   

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ID   D3P581_AZOS1            Unreviewed;       761 AA.
AC   D3P581;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Cellulose synthase catalytic subunit [UDP-forming] {ECO:0000256|RuleBase:RU365020};
DE            EC=2.4.1.12 {ECO:0000256|RuleBase:RU365020};
GN   OrderedLocusNames=AZL_c05170 {ECO:0000313|EMBL:BAI75810.1};
OS   Azospirillum sp. (strain B510).
OG   Plasmid pAB510c {ECO:0000313|EMBL:BAI75810.1,
OG   ECO:0000313|Proteomes:UP000002040}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI75810.1, ECO:0000313|Proteomes:UP000002040};
RN   [1] {ECO:0000313|EMBL:BAI75810.1, ECO:0000313|Proteomes:UP000002040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B510 {ECO:0000313|EMBL:BAI75810.1,
RC   ECO:0000313|Proteomes:UP000002040};
RC   PLASMID=pAB510c {ECO:0000313|EMBL:BAI75810.1};
RX   PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA   Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA   Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y.,
RA   Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N.,
RA   Nakayama S., Yamada M., Tabata S., Sato S.;
RT   "Complete genomic structure of the cultivated rice endophyte Azospirillum
RT   sp. B510.";
RL   DNA Res. 17:37-50(2010).
CC   -!- FUNCTION: Catalytic subunit of cellulose synthase. It polymerizes
CC       uridine 5'-diphosphate glucose to cellulose.
CC       {ECO:0000256|RuleBase:RU365020}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC         beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-
CC         COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00000122,
CC         ECO:0000256|RuleBase:RU365020};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU365020};
CC   -!- PATHWAY: Glycan metabolism; bacterial cellulose biosynthesis.
CC       {ECO:0000256|RuleBase:RU365020}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; AP010949; BAI75810.1; -; Genomic_DNA.
DR   RefSeq; WP_012977619.1; NC_013857.1.
DR   AlphaFoldDB; D3P581; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   KEGG; azl:AZL_c05170; -.
DR   HOGENOM; CLU_011907_0_0_5; -.
DR   OrthoDB; 9806824at2; -.
DR   UniPathway; UPA00694; -.
DR   Proteomes; UP000002040; Plasmid pAB510c.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
DR   GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro.
DR   CDD; cd06421; CESA_CelA_like; 1.
DR   Gene3D; 2.40.10.220; predicted glycosyltransferase like domains; 1.
DR   InterPro; IPR003919; Cell_synth_A.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR009875; PilZ_domain.
DR   NCBIfam; TIGR03030; CelA; 1.
DR   PANTHER; PTHR43867; CELLULOSE SYNTHASE CATALYTIC SUBUNIT A [UDP-FORMING]; 1.
DR   PANTHER; PTHR43867:SF2; CELLULOSE SYNTHASE CATALYTIC SUBUNIT A [UDP-FORMING]; 1.
DR   Pfam; PF13632; Glyco_trans_2_3; 1.
DR   Pfam; PF07238; PilZ; 1.
DR   PRINTS; PR01439; CELLSNTHASEA.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   4: Predicted;
KW   c-di-GMP {ECO:0000256|RuleBase:RU365020};
KW   Cell inner membrane {ECO:0000256|RuleBase:RU365020};
KW   Cell membrane {ECO:0000256|RuleBase:RU365020};
KW   Cellulose biosynthesis {ECO:0000256|ARBA:ARBA00022916,
KW   ECO:0000256|RuleBase:RU365020};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU365020};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365020};
KW   Plasmid {ECO:0000313|EMBL:BAI75810.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002040};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365020};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU365020};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU365020}.
FT   TRANSMEM        32..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   TRANSMEM        61..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   TRANSMEM        85..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   TRANSMEM        124..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   TRANSMEM        543..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   TRANSMEM        578..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   DOMAIN          265..484
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF13632"
FT   DOMAIN          603..706
FT                   /note="PilZ"
FT                   /evidence="ECO:0000259|Pfam:PF07238"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   761 AA;  84772 MW;  78B9898F9D5719EC CRC64;
     MTTSSDAKTV VRPMNNRAQQ TKRQASLNNR RFSLRSVLLW ILLLLSAGLF LALAALPVGR
     FASAAISAGV VVAAFVLGRF SQRFWHARTL TVLLLAFVTF RYFFWRLTGT LPPGDDLVNF
     VPGVTLFAAE ALSFVLFLTS LFVIIDPLER EPAAPTGDPA SWPSVDVYIP SYNEEPELLE
     TTLAAAVSID YPRDKLTVYL LDDGGTDQKL AQANPELAAA AKERRETLTA LCERLHVIYM
     SRPRNEHAKA GNINHAFQKT SGDLVLILDA DHVPTVGILK ATVGFFQRDS GLFLVQTPHF
     FVNPDPVEYN LGTFERMPSE NEMFYYSIQP GLDRWNGSFF CGSAAILRRA ALEEVGGFSG
     DTVTEDCETA LELHARGWRS VYLPRPLIAG LQPETFDSFI AQRSRWTQGM VQLFLLKNPL
     FKRGLTIAQR LCYLSTMMYW FFWFWRPIFL LSPLCYALFG LEIYRINLPD FACFVIPHVF
     AAAFLSQFLH GRMRWPLFSE LYEYLQSFHV SRAALATMIR PRDPVFKVTA KGQSVEGDGF
     SPLATPFIVT TLLLTAGLVA CGWRYYLFPE HRAAIVPVAV WCSLSLLLAL GGLAVVYERK
     RVRRQERFTV DRPAVLKFAD GTSIDLTVAD VSAGGVGLVV EPSWRDLLSL PDQTPVLTIA
     ATETEAATTT GVRISRIEPR NGELAVGAGF APRDRQDIVE MARFVFGNSV GWDSVLDRKR
     VAAPTFFGGL LFFATRVVPR LGHVLLALPG ALRRILTFQA P
//

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