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Database: UniProt
Entry: H1HM69_9BACT
LinkDB: H1HM69_9BACT
Original site: H1HM69_9BACT 
ID   H1HM69_9BACT            Unreviewed;       543 AA.
AC   H1HM69;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Extracellular endo-alpha-(1->5)-L-arabinanase C-terminal domain-containing protein {ECO:0000259|Pfam:PF16369};
GN   ORFNames=HMPREF9944_01263 {ECO:0000313|EMBL:EHO70789.1};
OS   Segatella maculosa OT 289.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Segatella.
OX   NCBI_TaxID=999422 {ECO:0000313|EMBL:EHO70789.1, ECO:0000313|Proteomes:UP000003167};
RN   [1] {ECO:0000313|EMBL:EHO70789.1, ECO:0000313|Proteomes:UP000003167}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT 289 {ECO:0000313|EMBL:EHO70789.1,
RC   ECO:0000313|Proteomes:UP000003167};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA   Mathney J., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA   McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella maculosa OT 289.";
RL   Submitted (DEC-2011) 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:EHO70789.1}.
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DR   EMBL; AGEK01000024; EHO70789.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1HM69; -.
DR   STRING; 999422.HMPREF9944_01263; -.
DR   PATRIC; fig|999422.3.peg.1304; -.
DR   HOGENOM; CLU_009397_1_3_10; -.
DR   OrthoDB; 9801455at2; -.
DR   Proteomes; UP000003167; 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; cd08998; GH43_Arb43a-like; 1.
DR   Gene3D; 2.40.128.10; -; 1.
DR   InterPro; IPR032291; Abn2_C.
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; PF16369; GH43_C; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|RuleBase:RU361187};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003167};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..543
FT                   /note="Extracellular endo-alpha-(1->5)-L-arabinanase C-
FT                   terminal domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003550515"
FT   DOMAIN          436..540
FT                   /note="Extracellular endo-alpha-(1->5)-L-arabinanase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16369"
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        310
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            243
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   543 AA;  61971 MW;  60DA9CF344F09BEA CRC64;
     MKTNSMVWIS FLAAIAFAGC KEDDNIEYEN PGSKVQTDVT VTDGQNMADD YTPIADWGNR
     FRWNLANVHD PSVVRADDGY YYMYQTDASY GNAHAGEGQS RGHFYCRRSK DLINWEFMGP
     TLHGVPTWVK SKLNEIRKDM GLAPSSIDFH NQTQFGFWAP CVRRIRRDLY RMYYVVTLPG
     TINGTGTWSE RCFIGLMETS NPADIDTWTD KGYVITNYSD RGLDFKVNAT DYARCYFKYN
     AIDPSLLINE KGEHWLVYGS WHSGFAALQL DPVTGKPLHA LGNPWGAENE TAYGKLIYTR
     KFGDRWQASE APEVVWHEGY YYLFMAYDEL SVAYNTRVVR SRNIEGPYYD ITGRDVTNRG
     GDAYPILTHP YRFGSDHGWV GISHCAVFND DKGNWYYASQ QRFPENYKGN AGSNALMVGG
     VRAIVWTSDG WPLVLPERYA GIAQKTISES ELLGDWQHIN LVYNYKRQDA SVSMTLAANH
     TVKSGWKTGK AWRFDASKNV LTIDNEQFYL RRELDWEANP RKATIVYVGL SSNGKTTYWG
     KKV
//
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