ID A0A124JZ56_9SPHN Unreviewed; 481 AA.
AC A0A124JZ56;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:KUR79384.1};
GN ORFNames=AQZ49_05495 {ECO:0000313|EMBL:KUR79384.1};
OS Novosphingobium sp. FSW06-99.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1739113 {ECO:0000313|EMBL:KUR79384.1, ECO:0000313|Proteomes:UP000061032};
RN [1] {ECO:0000313|EMBL:KUR79384.1, ECO:0000313|Proteomes:UP000061032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSW06-99 {ECO:0000313|EMBL:KUR79384.1,
RC ECO:0000313|Proteomes:UP000061032};
RA Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA Glaeser S.;
RT "Draft genome sequence of Novosphingobium sp. FSW06-99 (=LMG 27919), a
RT Novosphingobium acidiphilum related species isolated from a surface water
RT sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC {ECO:0000256|ARBA:ARBA00004834}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUR79384.1}.
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DR EMBL; LLZQ01000005; KUR79384.1; -; Genomic_DNA.
DR RefSeq; WP_067613783.1; NZ_KQ954253.1.
DR AlphaFoldDB; A0A124JZ56; -.
DR STRING; 1739113.AQZ49_05495; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000061032; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd08998; GH43_Arb43a-like; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR Pfam; PF14200; RicinB_lectin_2; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:KUR79384.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000061032};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..481
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007175001"
FT DOMAIN 375..444
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|Pfam:PF14200"
FT ACT_SITE 33
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 186
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 139
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 481 AA; 51589 MW; 744908DC358D033A CRC64;
MKAFLPALGL AAALMSGPAR AGDQLAGEPY IHDPSTITFS DGAYYTFGTG KGGLVSKDGW
TWHRGGERPG GGVAPDVIKI GDRYYVAYAV GGGGMNGGHA SNVRIMWTHS LDPASPDFGY
HDVGTVASSD GTEDCDAIDP AFLYVKGHWW LSYGTYFGYI RMVELDPATG QRLAGNTPVN
IAIDLEATAL MYRDGWYYLL GTQGTCCDGP NSTYNIRVGR SRDPLGPYVD NFGVPMLKGG
GKLVWGAHGR GYGAGHFGLV DLGDGVQKFS FHYESDMDRS GRSVLAIQPL LWNDGWPVGS
ENLRPGTYEI QSERGGALEL AVDAPRLPFD WRRSGFMAPD GPVAHLPDQT LAENQASWPA
GPIAVDMGAY MVRPHQHWTI TPVDGAGGYF GTPYVKITVA GTDRALATTA QGEITTVPAF
TGAPDQLWRL DQLTDGTYRI VPRAMPAEVT PLALTAVGRS TVRLARFNPD SAAARWTVHL
P
//
