AGL14_HALVD
ID AGL14_HALVD Reviewed; 300 AA.
AC D4GU71; L9V9H5;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Probable low-salt glycan biosynthesis reductase Agl14;
DE EC=1.1.1.-;
GN Name=agl14; OrderedLocusNames=HVO_2058;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=24194539; DOI=10.1128/mbio.00716-13;
RA Kaminski L., Guan Z., Yurist-Doutsch S., Eichler J.;
RT "Two distinct N-glycosylation pathways process the Haloferax volcanii S-
RT layer glycoprotein upon changes in environmental salinity.";
RL MBio 4:E00716-E00716(2013).
CC -!- FUNCTION: Reductase involved in N-glycan biosynthetic pathway that
CC takes place under low-salt conditions (1.75 M instead of 3.4 M).
CC Participates in the formation of the tetrasaccharide present at 'Asn-
CC 532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2
CC hexoses and rhamnose. Involved in the addition of final rhamnose (sugar
CC 4) of the tetrasaccharide on the dolichol phosphate carrier.
CC {ECO:0000269|PubMed:24194539}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:24194539}.
CC -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC {ECO:0000269|PubMed:24194539}.
CC -!- DISRUPTION PHENOTYPE: Impaired formation of the tetrasaccharide present
CC at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47' and
CC 'Asn-117' glycosylation of S-layer glycoprotein Csg.
CC {ECO:0000269|PubMed:24194539}.
CC -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ELY33652.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP001956; ADE02982.1; -; Genomic_DNA.
DR EMBL; AOHU01000040; ELY33652.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_013035334.1; NZ_AOHU01000040.1.
DR AlphaFoldDB; D4GU71; -.
DR SMR; D4GU71; -.
DR STRING; 309800.C498_05578; -.
DR EnsemblBacteria; ADE02982; ADE02982; HVO_2058.
DR EnsemblBacteria; ELY33652; ELY33652; C498_05578.
DR GeneID; 8924195; -.
DR KEGG; hvo:HVO_2058; -.
DR PATRIC; fig|309800.29.peg.1082; -.
DR eggNOG; arCOG01367; Archaea.
DR HOGENOM; CLU_045518_2_1_2; -.
DR OMA; AGETTWH; -.
DR OrthoDB; 43377at2157; -.
DR BioCyc; MetaCyc:MON-18754; -.
DR BRENDA; 1.1.1.133; 2561.
DR UniPathway; UPA00378; -.
DR UniPathway; UPA00977; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0045232; P:S-layer organization; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029903; RmlD-like-bd.
DR PANTHER; PTHR10491; PTHR10491; 1.
DR Pfam; PF04321; RmlD_sub_bind; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01214; rmlD; 1.
PE 3: Inferred from homology;
KW NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..300
FT /note="Probable low-salt glycan biosynthesis reductase
FT Agl14"
FT /id="PRO_0000428777"
FT ACT_SITE 135
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 10..12
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 11..12
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 46..47
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 46..47
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 70..72
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 70..72
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 109
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 135
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 135
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 139
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 139
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
SQ SEQUENCE 300 AA; 31977 MW; AFA61A0D91AF8F7F CRC64;
MYAFVTGANG LLGSVVVRTL REQGHAVVGS YHSEEPTFDC PLHQVDITDT ERVVELLDEY
DVDLVINCAA YTDVDGCESN PEVATAVNGT APGDLAAVCD DREIPFIHYS TDYVFDGETD
GFYEEGDEPA PIQEYGRSKL TGEHAVRDVN PDALILRLSF VYGARGDTSD LVGFPQWVAS
TLAAGDTVPL FTDQTMTPSR AGNVATTTLE LLDAGVSGTF HVASQSAVTP SDFGEKICEV
IGGDATLIES SVMADLDRPA ARPRRSCLDV SNVEGELGCS QPTLEDDLAA LEAAFSDYSS
