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
//