ALGI_AZOVI
ID ALGI_AZOVI Reviewed; 499 AA.
AC O52196;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Probable alginate O-acetylase AlgI;
DE EC=2.3.1.-;
DE AltName: Full=Alginate biosynthesis protein AlgI;
GN Name=algI;
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 9046;
RX PubMed=10352233; DOI=10.1016/s0378-1119(99)00119-5;
RA Vazquez-Ramos A., Moreno S., Guzman J., Alvarado A., Espin G.;
RT "Transcriptional organization of the Azotobacter vinelandii algGXLVIFA
RT genes: characterization of algF mutants.";
RL Gene 232:217-222(1999).
CC -!- FUNCTION: Together with AlgJ and AlgF, forms an inner membrane complex
CC which probably interacts with the alginate polymerization-transport
CC complex and adds acetyl groups at the O-2 and O-3 positions of
CC mannuronate residues. Acetylation of alginate increases cyst resistance
CC to desiccation.
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
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; AF027499; AAC04568.1; -; Genomic_DNA.
DR RefSeq; WP_012699741.1; NZ_FPKM01000036.1.
DR AlphaFoldDB; O52196; -.
DR SMR; O52196; -.
DR OMA; IIWGAWH; -.
DR UniPathway; UPA00286; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR024194; Ac/AlaTfrase_AlgI/DltB.
DR InterPro; IPR028362; AlgI.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
DR PIRSF; PIRSF500217; AlgI; 1.
DR PIRSF; PIRSF016636; AlgI_DltB; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Alginate biosynthesis; Cell inner membrane; Cell membrane;
KW Membrane; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..499
FT /note="Probable alginate O-acetylase AlgI"
FT /id="PRO_0000213123"
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 322
FT /evidence="ECO:0000255"
SQ SEQUENCE 499 AA; 56387 MW; CBB74AE4DF08F63C CRC64;
MVFSSNVFLF LFLPLFLGLY YLSPARYRNL LLLTASYVFY AWWRIDFLGL FAAVTVFNYW
IGLRIGAAGV RTQSAQRWLT LGVVVDLCVL GYFKYANFGV DSLNAIITSF GVEPFVVTHI
LLPIGISFYV FESISYIIDV YRGDTPATRN LVDFAAFVAI FPHLIAGPVL RFRDLVDQFN
HRTHTLDKFA EGCTRFMQGF IKKVFIADSL APIADHCFAL SDPTTGDAWL GALAYTAQLY
FDFSGYSDMA IGLGLMIGFR FMENFNQPYI SQSITEFWRR WHISLSTWLR DYLYISLGGN
RGTTFQTYRN LILTMLLGGL WHGANWTFII WGAWHGTWLA IERALRIDAA PKTIRPLRWV
FAFLLVMVGW VIFRAENLDV AWRMYAAMFS FGDWTLSDLN KAQLTSLQIA TLLLAYVVIA
VYGIRQFYAQ PLTGAPKAKA NDQADAPQGI VHASSGTLAY SQAIDIPALA TRVAVLLLFA
ASVLKLSAQS FSPFLYFQF