ID A0A0M2HPI6_9MICO Unreviewed; 325 AA.
AC A0A0M2HPI6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Intracellular endo-alpha-(1->5)-L-arabinanase {ECO:0000313|EMBL:KJL48667.1};
DE EC=3.2.1.99 {ECO:0000313|EMBL:KJL48667.1};
GN Name=abn-ts {ECO:0000313|EMBL:KJL48667.1};
GN ORFNames=RS84_00834 {ECO:0000313|EMBL:KJL48667.1};
OS Microbacterium hydrocarbonoxydans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=273678 {ECO:0000313|EMBL:KJL48667.1, ECO:0000313|Proteomes:UP000033900};
RN [1] {ECO:0000313|EMBL:KJL48667.1, ECO:0000313|Proteomes:UP000033900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA35 {ECO:0000313|EMBL:KJL48667.1,
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, ECO:0000256|PIRNR:PIRNR026534}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|PIRNR:PIRNR026534}.
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:KJL48667.1}.
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DR EMBL; JYJB01000006; KJL48667.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2HPI6; -.
DR STRING; 273678.RS84_00834; -.
DR PATRIC; fig|273678.4.peg.828; -.
DR UniPathway; UPA00667; -.
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:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd08998; GH43_Arb43a-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR016840; Glyco_hydro_43_endo_a_Ara-ase.
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; PF04616; Glyco_hydro_43; 1.
DR PIRSF; PIRSF026534; Endo_alpha-L-arabinosidase; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR026534};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR026534};
KW Reference proteome {ECO:0000313|Proteomes:UP000033900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..325
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038792293"
FT ACT_SITE 39
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-1"
FT ACT_SITE 216
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-1"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 159..162
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 179..181
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT SITE 162
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 325 AA; 34930 MW; D2FA889E368295A8 CRC64;
MISRRSRPAA AAAALVAVAA VLVGCSGAPS LSGDVFVHDP AYVHTDHGDF VYSTGNGQVG
DGNVQIRRSD DGASWEHVGE VWKTKPEWLS DAVPGVDNLW APELYEHDGT WYMYYAASTF
GSNRSVIALA TNSTLDPADP DYEWVDRGEV IGSEGTDFNA IDAGIVEDAQ GVPWMSFGSF
WSGIRMVELE WPSGLRADDA EPLRLADRGT AENAIEAPYI VAHDGWFYLF ASRGFCCRGV
DSTYEIIVGR SRDVTGPYLD RDGVSLLEDG GTVVLGSEGS RIGPGGQSVS NGTLAFHFYD
ADAAGIPTLG LRPITWRDGW PTVAR
//
