ID Q0HV90_SHESR Unreviewed; 1121 AA.
AC Q0HV90;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Glycoside hydrolase, family 43 {ECO:0000313|EMBL:ABI42965.1};
GN OrderedLocusNames=Shewmr7_1976 {ECO:0000313|EMBL:ABI42965.1};
OS Shewanella sp. (strain MR-7).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60481 {ECO:0000313|EMBL:ABI42965.1};
RN [1] {ECO:0000313|EMBL:ABI42965.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MR-7 {ECO:0000313|EMBL:ABI42965.1};
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 Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of Chromosome1 of Shewanella sp. MR-7.";
RL Submitted (AUG-2006) 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}.
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DR EMBL; CP000444; ABI42965.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0HV90; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR KEGG; shm:Shewmr7_1976; -.
DR HOGENOM; CLU_009397_1_1_6; -.
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; 2.40.128.10; -; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR InterPro; IPR046780; aBig_2.
DR InterPro; IPR032291; Abn2_C.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR Pfam; PF20578; aBig_2; 2.
DR Pfam; PF16369; GH43_C; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR Pfam; PF13385; Laminin_G_3; 2.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
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:ABI42965.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1121
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004173349"
FT DOMAIN 392..501
FT /note="Extracellular endo-alpha-(1->5)-L-arabinanase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF16369"
FT DOMAIN 525..594
FT /note="Atrophied bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF20578"
FT DOMAIN 831..910
FT /note="Atrophied bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF20578"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 256
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 203
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 1121 AA; 120754 MW; A14D09B0ACCCDCDE CRC64;
MVLKRSFVSA SLIMALASCG GDDSSYSAND TNTFTPPAPA TSADPTIAGE VSYKNAVVHD
PSIIKDTDGT YYVFGSHLAV ASSTDLMNWT QIASDGVPES SLFNTYESEI AEGTAWTGGF
VGSWAPDVIK LADGKYHFYY DFCGGPDKID CVSRSYLGMA TSDNILGPYV NQGLILKSGH
EGAENPGANG QIYDGFVDPN AIDPAVFYDK DGGLWMTYGS YSGGIWVMQL DPATGLPLEG
QGYGTKIMGG NYSAIEGSYV IYSPESEYYY MFTSFGGFAQ KDGYNIRISR SKNPNGPYVD
AAGLDMIGAT AAGNIADYGV KLMGGFQFVA HPGDVGHDHG YLSPGHNSAF YDAQTGKYFL
VFHTRFPDTG EGHSVRVHEL FLNSDGWLVA SPQRYAPING DNIVDEIDVT GDYQFINHAK
NINTAAHTSL HIKLSRTWTN KGSVSGDVTG TYQQGDDNQI TLMLDNLGTF EGVLAWQWDP
EQNKLMPTFS AISNDGVSIW GVKLTDNTTE EILSASANGI SLPTEVTEGT LALPTQGTRG
STIEWQSSDE SVIRADGTII RPNVGEGDKV VTLTATIMVN GKKVTKTFQI TVFAHKTYNR
IAQYSFENNL KDSLGLFGDG QPTGDRIFKA GDTIGYATGF EGQALSLDGA HGVLLPSGII
SSYEYTVSFW ASPAVITGFT TAFFGAVNEQ TAEDASKFSN TWVSLLPQGW DGNTMFWSHN
IDTSGSSVLE TWFDGVTGER IAENTWSHLA FSVNKGLVKV FINGVERFSS GNLANYFTGA
QGVFGLGVNY WDVPYNGLID ELKVYEAALT AEEVKALDID KLADSELLSS ATAILELGDL
SAVRENIELP VTGPYASAIT WVSSDPTIID TRGTVNQPGR EETDKVVTLT ATLKLGQATQ
TKVFTATVKS KAPPTPVAVY SFEENLNDST ANFGAGTVVG NLIGVEGGKI SYVDGAVGKA
AVFDGASGIV LPNNLIKDYT YSVSMWLNPE QLNKYTTALF GYATDSSWTS VLPGGQNDYE
RMVLWSGTAW YDGRTGFVMP KSQWTHLAYT VNGGDVKVYI NGELKFTGAN FPNIFSVPTT
KFAVGVNFWD TPFKGAIDEI KFYDEAITEQ DVADLFGESN Q
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