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Database: UniProt
Entry: A0A0M2HX36_9MICO
LinkDB: A0A0M2HX36_9MICO
Original site: A0A0M2HX36_9MICO 
ID   A0A0M2HX36_9MICO        Unreviewed;       790 AA.
AC   A0A0M2HX36;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Extracellular endo-alpha-(1->5)-L-arabinanase 2 {ECO:0000313|EMBL:KJL49490.1};
DE            EC=3.2.1.99 {ECO:0000313|EMBL:KJL49490.1};
GN   Name=abn2 {ECO:0000313|EMBL:KJL49490.1};
GN   ORFNames=RS84_00203 {ECO:0000313|EMBL:KJL49490.1};
OS   Microbacterium hydrocarbonoxydans.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=273678 {ECO:0000313|EMBL:KJL49490.1, ECO:0000313|Proteomes:UP000033900};
RN   [1] {ECO:0000313|EMBL:KJL49490.1, ECO:0000313|Proteomes:UP000033900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA35 {ECO:0000313|EMBL:KJL49490.1,
RC   ECO:0000313|Proteomes:UP000033900};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-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}.
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:KJL49490.1}.
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DR   EMBL; JYJB01000003; KJL49490.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M2HX36; -.
DR   STRING; 273678.RS84_00203; -.
DR   PATRIC; fig|273678.4.peg.193; -.
DR   OrthoDB; 9801455at2; -.
DR   Proteomes; UP000033900; Unassembled WGS sequence.
DR   GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd18832; GH43_GsAbnA-like; 1.
DR   Gene3D; 2.40.128.10; -; 1.
DR   Gene3D; 2.60.120.200; -; 1.
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; 1.
DR   Pfam; PF16369; GH43_C; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   Pfam; PF13385; Laminin_G_3; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:KJL49490.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KJL49490.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033900};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..790
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018282165"
FT   DOMAIN          383..486
FT                   /note="Extracellular endo-alpha-(1->5)-L-arabinanase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16369"
FT   DOMAIN          500..580
FT                   /note="Atrophied bacterial Ig"
FT                   /evidence="ECO:0000259|Pfam:PF20578"
FT   ACT_SITE        48
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        237
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            184
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   790 AA;  83263 MW;  CEE542C625B983A5 CRC64;
     MPRTARISIA LAAAAALTMG CLTASPAWAK PPSSAPAPPD FNDVSVHDPS IVTSGDTIWA
     FGSHGASAHT TDLIDWQQYT VDLSQNPDNA LFDDIYTELA DTFDWAQTST LWAADVIQLP
     DGRYAMYYNA CEGSSPRSAL GIATSDAVDG PYENQGILLK SGMSGESENS GEVYDAHVHP
     NTVDPDAFYD ADGNMWMVYG SYSGGIFILK LDPTTGEPLP GQGYGKHLVG GNHSRIEAPT
     IQYNPATGYY YLYLSFGGLD ASGGYNVRVA RSTSPDGPYL DADGNDMADV KADPSLPLFD
     DASVQPYGVK LMGSYLFDRE LGDPGTGTGI GYNSPGHNSW YQDPETGRMF LVFHARFPGS
     GEHHEVRVHQ IYMNADGWPV ISPQRYAGET AGKIVRDDVV GSWQLVNMGK DITAVPAAST
     DISLTRNGRI TGDSTGTWKL TGQHDATLTI DGETYKGEFV PVWDLALEKW STGFTALSPH
     GVAVWGRLVP TISPADAVTA VASAIDLGDT SAVTADLNLP TEGTSGTTIS WATSDAGVVT
     SAGVVTRPAI GSSDAHATLT ATIRNADATK SLAFDVTVLA RAPGVISGTW SFENDLSDAT
     GQHPAATATG PRLDAAGGTI SYADDGVRGS ALHLDGSSGV RLPNELIHGS EYTVSVWLRP
     EHLTAYTSAF FGAAGPESWV SLVPQGHSGV GGSTMVWSGT AWYDAGTGMS MPLDRWSHVA
     FVVDHGAVSV FIDGVKKFQG SGFPDVLSAP GAQFGIGVNW WDTPFQGDVD ELSVWSSALS
     PEDIAGLAAR
//
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