ID A0A0M8VF28_9ACTN Unreviewed; 1739 AA.
AC A0A0M8VF28;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Hydrolase {ECO:0000313|EMBL:KOV61383.1};
GN ORFNames=ADL01_31170 {ECO:0000313|EMBL:KOV61383.1};
OS Streptomyces sp. NRRL WC-3618.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV61383.1, ECO:0000313|Proteomes:UP000037738};
RN [1] {ECO:0000313|EMBL:KOV61383.1, ECO:0000313|Proteomes:UP000037738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV61383.1,
RC ECO:0000313|Proteomes:UP000037738};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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:KOV61383.1}.
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DR EMBL; LGDW01000452; KOV61383.1; -; Genomic_DNA.
DR RefSeq; WP_053745333.1; NZ_LGDW01000452.1.
DR PATRIC; fig|1519490.3.peg.6798; -.
DR OrthoDB; 9758923at2; -.
DR Proteomes; UP000037738; 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:UniProtKB-KW.
DR CDD; cd08983; GH43_Bt3655-like; 1.
DR CDD; cd09004; GH43_bXyl-like; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.40.2340; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR046780; aBig_2.
DR InterPro; IPR011081; Big_4.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF20578; aBig_2; 2.
DR Pfam; PF07532; Big_4; 1.
DR Pfam; PF04616; Glyco_hydro_43; 2.
DR Pfam; PF13385; Laminin_G_3; 2.
DR SMART; SM00560; LamGL; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF49299; PKD domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KOV61383.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000037738};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..41
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 42..1739
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005826163"
FT DOMAIN 908..1050
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT REGION 1507..1537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1154
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 1313
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 1266
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 1739 AA; 183901 MW; 6916342ACCFC2CB7 CRC64;
MQLARSRDRS RPWSERLAGL TAASLLLGLA GPLAMSVPAH AAAAGVTDGL ALWYKLDAAS
GTTVADASGN GRTGTVNGTA GWSNSGDGLA FNGSNTYIKV PDNIMSGMSS ITVAMDVKID
AAQANPYFIY GFGNTVGTAG NGYLFTTGNS YRTSIASGNW STEQNTRSAG TNLQRAVWKQ
ITYTQTGTTG VLYEDGVEVG RNTAVTITPG SIGAGTTTAN YIGKSVYPGD NLFKGNIRDF
RVYNRALAST EVEELSLPIA AQGVAADKSA LTLGDTSAVT ADLTLPSAGP AGGSAITWAT
DNASVVSASG AVTRPAAGQP DGHATLTATL KKGPASDTKT FDITVPATFD DTTATQQAAD
ALTVPNIDDV RGNITLPSTG AYGTAVAWSS ANPDVIAADG VVHRPAHGAG GTTVDLTATI
TKGTATATRA FTAKVPELPA KEALKGYMFS YFTGEGTSDG EQLYAALSKG NDPLKWRELN
NGKPVLTSTL GEKGLRDPFI IRSPEGDKFY QIATDLRIYG NGDWDASQRT GSKSIMVWES
TDLVHWTDQR LVKVSPDSAG NTWAPEAFYD AKLGSYVVFW ASKLYDNADH SGDTYNRMMY
ATTRDFRTFS APKVWIDRGY SVIDSTMIKD SDTYYRFSKD ERNNTSSTPN SKFIFEEKSD
SILNPSYDFV AEGIGKGAMS AAEGPLVFKS NTEKKWYMFA DEFGGRGYIP FESTDLASGV
WTPSTNYDLP SKPRHGTVLP VTQAEYDRLL STYQPDQIIT SAENVKVETR IGEAPVLPAT
VIAESGDGVK RPVAVTWASV DASQYAQAGT FTVTGDLAGD SAIAVSAEIT VSAEGPDVPA
DLLLHYDFDE TGGSIVRDSS GHGYHGTYVR TPAFGTGVHG GSFKMSGGNS SSSSPYVKIP
GGVLKDATGV TVSTYVKWKG GDNFQWLFGL GPDSNRYLFA TPSNGAGKLF SAITKATWSG
EKQMIGGSPL TAGEWQHVTV TLDGATETAI LYVNGAETAR VSGVTIKPSD LYDASKDYSG
YIGKSLYSPD PYFGGEVDDF RIYNRALTPA EVLRLGGNTT GIANVTHPAL KVDAIINDKD
SKVVLPLNPG SDVRALAPQF TLAHGASISP ASGTLRDFSK PLTYEVTGSD GKKRTWTVSA
VEMKSPVLPG LNADPNIVRF GDTFYIYPTT DGFEGWSGTQ FKAYSSTDLV HWKDHGVILD
LGPDISWADS RAWAPTMEER NGKYYFYFCA DANIGVAVSD SPTGPFKDAL GKPLLKAGDH
PGQMIDPAVF TDDDGQSYLY WGNGRAYVVP LNNDMVSFDP SKVTDITPSG YNEGSFVIKR
GATYYFMWSE NDTRDENYQV AYATGSSPTG PWTKRGVILE KDLSLGIKGT GHHSVVHVPN
TDDWYIAYHR FAIPGGDGMH RETTIDKLEF DADGLIKKVV PTLSSIDPVT IVHAGADTTG
QEGSAIPLTG SISGAGTPSW SVGAATPCTF SSPTMVPTTI TCRDNGTYEV TLTGGRSKDT
LTVTVSNAPP SITSVQGPKA PVPAGRSTPA RVSAKFTDPG LADTHTCRID WKDGTTPTAG
KVTGGTCEAS HAYLKAGILR PTITVTDDDG ATATAQLPEL IVFDPAAGSA KGKGVIPSRA
GSYPADPRLT GKAAFSFGAS YPKGATVPKG ATSFDFTAAG ASKATVQLRA KSSDWLVVTG
STAVFQGSGT VNGKSGYVFR VTATDKPDTF RIRIWQKTTG DVVYDNRTGA ATKDIVIGR
//
