ID A4XF17_NOVAD Unreviewed; 888 AA.
AC A4XF17;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Glycoside hydrolase family 2, sugar binding {ECO:0000313|EMBL:ABP64528.1};
GN OrderedLocusNames=Saro_3669 {ECO:0000313|EMBL:ABP64528.1};
OS Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS 56034 / CIP 105152 / NBRC 16084 / F199).
OG Plasmid pNL2 {ECO:0000313|EMBL:ABP64528.1,
OG ECO:0000313|Proteomes:UP000009134}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=279238 {ECO:0000313|EMBL:ABP64528.1, ECO:0000313|Proteomes:UP000009134};
RN [1] {ECO:0000313|EMBL:ABP64528.1, ECO:0000313|Proteomes:UP000009134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084
RC / F199 {ECO:0000313|Proteomes:UP000009134};
RC PLASMID=pNL2 {ECO:0000313|EMBL:ABP64528.1,
RC ECO:0000313|Proteomes:UP000009134};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Han C., Thomson S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Ivanova N., Fredrickson J., Romine M.F., Richardson P.;
RT "Complete sequence of plasmid pNL2 of Novosphingobium aromaticivorans DSM
RT 12444.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; CP000677; ABP64528.1; -; Genomic_DNA.
DR RefSeq; WP_011906915.1; NC_009427.1.
DR AlphaFoldDB; A4XF17; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; nar:Saro_3669; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_006501_5_0_5; -.
DR Proteomes; UP000009134; Plasmid pNL2.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF16355; DUF4982; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABP64528.1};
KW Plasmid {ECO:0000313|EMBL:ABP64528.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009134};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..888
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002676810"
FT DOMAIN 33..195
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 216..316
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 325..638
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 665..720
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
SQ SEQUENCE 888 AA; 96354 MW; 56FF4A3098216629 CRC64;
MTLRSRSAGV SLMVLAFVAC PAFAQEVRTV SALESGWRFL DGDVAGAVAP DFADAAWEQV
EVPHTWNRVG FYRHDMGGAN TEANVRKRQG VGWYRLRFSP APVRPGDRSW LEFDAASRTA
QVWLNGTYLG EHRGGFSRFR LDATAVLRAG AENVLVVRVD NTQPAAGAPT ADVLPLTGDF
FVHGGLYRPV RLVTTAPLHI DMTDHGGAGI RAATVSASTG SARVKVAVRV ANDGRGSTRA
IARVALFDRD GREVAAARVP ATVASGKVAE VEAELSVAAP HLWQGTKDPY LHDLVTEVLD
KDGKVVDRIS QPFGIRTMTF DPERGFVLNG QPYRLKGVGY HQDRDGKGWA ISRADVAEDV
ATIREMGANT IRLTHYQHGQ DIHDLADRAG IVVWDEIPLV SAWTLGGKLD PDPALVANAR
QQLTELVRQN QNHAATAIWS IANEVDFGNS MPIFLTADAQ GRVADPMALL KELDGLAKAL
DPSRPTALAT CCEGNRQAPG TQIPITATAA DLGGANRYFG WYYGKPSELG AHLDKLRAGR
PDQPLSLTEY GAGGGLTIHT DNVLGGPADS RGFAQPEEYE SWVHEQTLPQ LDARPWLYAT
WLWNSFDFAT RIRTEGDAQD INTKGLVAYD HKTRKDAWYF YKANWNVEPM VHITAKRYKE
RAYPVTEVKV YSNTASTELL LNGRSLGTKS DCPAKVCVWN AVALDDGANA LVARGTHAGG
QVEDRAEWAL APETRRHMVI DAGTLVAGKG AGRILGSDNW FEGGSTATLD QPADFGKPGK
PAEIVGTQER DALATYRTGT FSYRVPVADG RYKVTLWFAT ASAQKPGTFE VRNGRKTLLR
KFQPAIPASG AVAEARAFTV RAKGTLALDF VPGSGDARVS MIEIERLR
//
