ID   ALGX_AZOVI              Reviewed;         483 AA.
AC   O52194;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Alginate biosynthesis protein AlgX;
DE   AltName: Full=Probable alginate O-acetyltransferase AlgX;
DE            EC=2.3.1.-;
DE   Flags: Precursor;
GN   Name=algX;
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: Plays two roles in the biosynthesis of the exopolysaccharide
CC       alginate: protects alginate from degradation as the polymer traverses
CC       the periplasm, and also plays a role in its O-acetylation. Probably has
CC       acetyltransferase activity in vivo (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- DOMAIN: Consists of two domains, with an N-terminal domain with
CC       structural homology to members of the SGNH (GDSL) hydrolase superfamily
CC       and a C-terminal carbohydrate-binding module (CBM) that may bind
CC       alginate. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AlgX family. {ECO:0000305}.
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DR   EMBL; AF027499; AAC04566.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52194; -.
DR   SMR; O52194; -.
DR   UniPathway; UPA00286; -.
DR   GO; GO:0042597; C:periplasmic space; 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   CDD; cd14487; AlgX_C; 1.
DR   CDD; cd14441; AlgX_N; 1.
DR   Gene3D; 2.60.120.1380; -; 1.
DR   InterPro; IPR031811; ALGX/ALGJ_SGNH-like.
DR   InterPro; IPR031798; AlgX_C.
DR   InterPro; IPR038639; AlgX_C_sf.
DR   InterPro; IPR034655; AlgX_N.
DR   Pfam; PF16822; ALGX; 1.
DR   Pfam; PF16824; CBM_26; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Alginate biosynthesis; Disulfide bond; Periplasm; Signal;
KW   Transferase.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..483
FT                   /note="Alginate biosynthesis protein AlgX"
FT                   /id="PRO_0000020670"
FT   REGION          27..349
FT                   /note="SGNH hydrolase-like domain"
FT   REGION          350..480
FT                   /note="CBM domain"
FT   ACT_SITE        177
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        179
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        271
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..232
FT                   /evidence="ECO:0000250"
FT   DISULFID        349..466
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   483 AA;  53996 MW;  5A5727B68317A1CC CRC64;
     MKTHNSKWIG PAALAAAIAL AAAGVRAEET PTGLPVYRAE SCCDLCPAAA DPNSYTSNYM
     KGFVTLVQGN ESDWLFRTNE DLRTEFGTTP EGYRQLKALH DAFKSRGVEL VIVYQPTRGM
     VQRNKLLPAD YARFDYDKAV RNFRATLKHF EQLGYWVPDL TPLTDEKVEP AFYFRGDHHW
     TSYGAERSAR IVAETVKEIP AFADIPRKEF VTKKMGRMGK RGTHHRVAGQ LCNTTYAFEH
     SDQFFTEPKG EGGGDLFGDS SLPQITLVGT SHSGTNYNFA GFLSEYMGAE ILNVAFPGSG
     LEGSMLKYLA SDEFQKNPPK ILIWEFSPLY DLAEDKFYRQ ALSMLGNACE GEKTLLAGKA
     TLRPGEAGKE VLINGAGRLV EATNSRHQVD IRFSDPSVKK LEGTIWYMTG RREKFQFDKP
     VTTETNGRFA FNMRDEADWG GLNFFAMEIQ PPEGLKEPVE VEVRLCKRHD YHAPANLTAR
     SGN