XYNA1_PAESJ
ID XYNA1_PAESJ Reviewed; 1462 AA.
AC C6CRV0; Q53I45;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Endo-1,4-beta-xylanase A;
DE EC=3.2.1.8;
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase A;
DE Flags: Precursor;
GN Name=xynA1; Synonyms=xynA; OrderedLocusNames=Pjdr2_0221;
OS Paenibacillus sp. (strain JDR-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=324057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=JDR-2;
RX PubMed=16461704; DOI=10.1128/aem.72.2.1496-1506.2006;
RA Stjohn F.J., Rice J.D., Preston J.F.;
RT "Paenibacillus sp. strain JDR-2 and XynA1: a novel system for
RT methylglucuronoxylan utilization.";
RL Appl. Environ. Microbiol. 72:1496-1506(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDR-2;
RX PubMed=22675593; DOI=10.4056/sigs.2374349;
RA Chow V., Nong G., St John F.J., Rice J.D., Dickstein E., Chertkov O.,
RA Bruce D., Detter C., Brettin T., Han J., Woyke T., Pitluck S., Nolan M.,
RA Pati A., Martin J., Copeland A., Land M.L., Goodwin L., Jones J.B.,
RA Ingram L.O., Shanmugam K.T., Preston J.F.;
RT "Complete genome sequence of Paenibacillus sp. strain JDR-2.";
RL Stand. Genomic Sci. 6:1-10(2012).
CC -!- FUNCTION: Catalyzes the depolymerization of methylglucuronoxylan
CC (MeGAXn), a beta-1,4 xylan in which 10% to 20% of the xylose residues
CC are substituted with alpha-1,2-4-O-methylglucuronate (MeGA) residues,
CC which is predominant in hemicellulose fractions of hardwood and crop
CC residues. Generates xylobiose (X2) and aldotetrauronate (MeGAX3) as the
CC predominant products of MeGAXn hydrolysis; these products are then
CC directly assimilated by the bacterium for subsequent metabolism. Thus,
CC allows the bacterium to efficiently use polymeric MeGAXn as a growth
CC substrate. {ECO:0000269|PubMed:16461704}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000269|PubMed:16461704};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=8.0 umol/min/mg enzyme with sweet gum methylglucuronoxylan as
CC substrate {ECO:0000269|PubMed:16461704};
CC pH dependence:
CC Optimum pH is 6.5 with sweet gum methylglucuronoxylan as substrate.
CC {ECO:0000269|PubMed:16461704};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius with sweet gum
CC methylglucuronoxylan as substrate. {ECO:0000269|PubMed:16461704};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:16461704}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000305}.
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DR EMBL; AJ938162; CAI79477.1; -; Genomic_DNA.
DR EMBL; CP001656; ACS98901.1; -; Genomic_DNA.
DR RefSeq; WP_012772223.1; NC_012914.1.
DR PDB; 3RDK; X-ray; 1.49 A; A/B=518-851.
DR PDB; 3RO8; X-ray; 1.34 A; A/B/C/D/E/F/G/H=518-851.
DR PDB; 4E4P; X-ray; 1.92 A; A/B=518-851.
DR PDBsum; 3RDK; -.
DR PDBsum; 3RO8; -.
DR PDBsum; 4E4P; -.
DR AlphaFoldDB; C6CRV0; -.
DR SMR; C6CRV0; -.
DR STRING; 324057.Pjdr2_0221; -.
DR CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR CAZy; CBM9; Carbohydrate-Binding Module Family 9.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR EnsemblBacteria; ACS98901; ACS98901; Pjdr2_0221.
DR KEGG; pjd:Pjdr2_0221; -.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_001408_1_0_9; -.
DR OMA; IARVTFW; -.
DR OrthoDB; 654705at2; -.
DR UniPathway; UPA00114; -.
DR GO; GO:0005618; C:cell wall; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IDA:UniProtKB.
DR GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
DR InterPro; IPR010502; Carb-bd_dom_fam9.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR001119; SLH_dom.
DR PANTHER; PTHR31490; PTHR31490; 1.
DR Pfam; PF06452; CBM9_1; 1.
DR Pfam; PF02018; CBM_4_9; 3.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR Pfam; PF00395; SLH; 3.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF49785; SSF49785; 3.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
DR PROSITE; PS51272; SLH; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell wall; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Repeat; Secreted; Signal; Xylan degradation.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1462
FT /note="Endo-1,4-beta-xylanase A"
FT /id="PRO_5000484609"
FT DOMAIN 64..165
FT /note="CBM-cenC 1"
FT DOMAIN 207..319
FT /note="CBM-cenC 2"
FT DOMAIN 360..490
FT /note="CBM-cenC 3"
FT DOMAIN 514..851
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT DOMAIN 1279..1342
FT /note="SLH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT DOMAIN 1345..1404
FT /note="SLH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT DOMAIN 1407..1462
FT /note="SLH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT ACT_SITE 651
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 706
FT /evidence="ECO:0000250"
FT ACT_SITE 775
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT CONFLICT 313
FT /note="S -> T (in Ref. 1; CAI79477)"
FT /evidence="ECO:0000305"
FT CONFLICT 454..461
FT /note="SLASKTIT -> TPTTQAWQARRLP (in Ref. 1; CAI79477)"
FT /evidence="ECO:0000305"
FT HELIX 520..523
FT /evidence="ECO:0007829|PDB:3RO8"
FT TURN 524..527
FT /evidence="ECO:0007829|PDB:3RO8"
FT STRAND 529..534
FT /evidence="ECO:0007829|PDB:3RO8"
FT HELIX 536..539
FT /evidence="ECO:0007829|PDB:3RO8"
FT HELIX 541..550
FT /evidence="ECO:0007829|PDB:3RO8"
FT STRAND 552..558
FT /evidence="ECO:0007829|PDB:3RO8"
FT HELIX 562..565
FT /evidence="ECO:0007829|PDB:3RO8"
FT HELIX 575..586
FT /evidence="ECO:0007829|PDB:3RO8"
FT STRAND 590..597
FT /evidence="ECO:0007829|PDB:3RO8"
FT STRAND 599..601
FT /evidence="ECO:0007829|PDB:3RO8"
FT HELIX 604..606
FT /evidence="ECO:0007829|PDB:3RO8"
FT STRAND 608..610
FT /evidence="ECO:0007829|PDB:3RO8"
FT STRAND 616..618
FT /evidence="ECO:0007829|PDB:3RO8"
FT HELIX 621..639
FT /evidence="ECO:0007829|PDB:3RO8"
FT HELIX 640..642
FT /evidence="ECO:0007829|PDB:3RO8"
FT STRAND 643..650
FT /evidence="ECO:0007829|PDB:3RO8"
FT HELIX 664..666
FT /evidence="ECO:0007829|PDB:3RO8"
FT HELIX 671..676
FT /evidence="ECO:0007829|PDB:3RO8"
FT HELIX 680..694
FT /evidence="ECO:0007829|PDB:3RO8"
FT STRAND 701..707
FT /evidence="ECO:0007829|PDB:3RO8"
FT HELIX 712..732
FT /evidence="ECO:0007829|PDB:3RO8"
FT TURN 733..735
FT /evidence="ECO:0007829|PDB:3RO8"
FT STRAND 741..744
FT /evidence="ECO:0007829|PDB:3RO8"
FT STRAND 747..749
FT /evidence="ECO:0007829|PDB:3RO8"
FT HELIX 754..765
FT /evidence="ECO:0007829|PDB:3RO8"
FT TURN 766..768
FT /evidence="ECO:0007829|PDB:3RO8"
FT STRAND 770..779
FT /evidence="ECO:0007829|PDB:3RO8"
FT HELIX 787..807
FT /evidence="ECO:0007829|PDB:3RO8"
FT HELIX 808..811
FT /evidence="ECO:0007829|PDB:3RO8"
FT STRAND 812..817
FT /evidence="ECO:0007829|PDB:3RO8"
FT HELIX 822..824
FT /evidence="ECO:0007829|PDB:3RDK"
FT HELIX 828..830
FT /evidence="ECO:0007829|PDB:3RDK"
FT STRAND 833..835
FT /evidence="ECO:0007829|PDB:3RDK"
FT HELIX 843..849
FT /evidence="ECO:0007829|PDB:3RDK"
SQ SEQUENCE 1462 AA; 157322 MW; AE29664CDEA3BF3E CRC64;
MSRSLKKFVS ILLAAALLIP IGRLAPVAEA AENPTIVYHE DFAIDKGKAI QSGGASLTQV
TGKVFDGNND GSALYVSNRA NTWDAADFKF ADIGLQNGKT YTVTVKGYVD QDATVPSGAQ
AFLQAVDSNN YGFLASANFA AGTAFTLTKE FTVDTSVSTQ LRVQSSEEGK AVPFYIGDIL
ITANPTTTTN TVYHEDFATD KGKAVQSGGA NLAQVADKVF DGNDDGKALY VSNRANTWDA
ADFKFADIGL QNGKTYTVTV KGYVDQDATV PSGAQAFLQA VDSNNYGFLA SANFAARSAF
TLTKEFTVDT SVSTQLRVQS SEEGKAVPFY IGDILITETV NSGGGQEDPP RPPALPFNTI
TFEDQTAGGF TGRAGTETLT VTNESNHTAD GSYSLKVEGR TTSWHGPSLR VEKYVDKGYE
YKVTAWVKLL SPETSTKLEL ASQVGDGGSA NYPSLASKTI TAADGWVQLQ GNYRYNSVGG
EYLTIYVQSS NATASYYIDD ISFESTGSGP VGIQKDLAPL KDVYKNDFLI GNAISAEDLE
GTRLELLKMH HDVVTAGNAM KPDALQPTKG NFTFTAADAM IDKVLAEGMK MHGHVLVWHQ
QSPAWLNTKK DDNNNTVPLG RDEALDNLRT HIQTVMKHFG NKVISWDVVN EAMNDNPSNP
ADYKASLRQT PWYQAIGSDY VEQAFLAARE VLDENPSWNI KLYYNDYNED NQNKATAIYN
MVKDINDRYA AAHNGKLLID GVGMQGHYNI NTNPDNVKLS LEKFISLGVE VSVSELDVTA
GNNYTLPENL AVGQAYLYAQ LFKLYKEHAD HIARVTFWGM DDNTSWRAEN NPLLFDKNLQ
AKPAYYGVID PDKYMEEHAP ESKDANQAEA QYGTPVIDGT VDSIWSNAQA MPVNRYQMAW
QGATGTAKAL WDDQNLYVLI QVSDSQLNKA NENAWEQDSV EVFLDQNNGK TTFYQNDDGQ
YRVNFDNETS FSPASIAAGF ESQTKKTANS YTVELKIPLT AVTPANQKKL GFDVQINDAT
DGARTSVAAW NDTTGNGYQD TSVYGELTLA GKGTGGTGTV GTTVPQTGNV VKNPDGSTTL
KPEVKTTNGN AVGTVTGDDL KKALDQAAPA AGGKKQVIID VPLQANAATY AVQLPTQSLK
SQDGYQLTAK IANAFIQIPS NMLANTNVTT DQVSIRVAKA SLDNVDAATR ELIGNRPVID
LSLVAGGNVI AWNNPTAPVT VAVPYAPTAE ELKHPEHILI WYIDGSGKAT PVPNSRYDAA
LGAVVFQTTH FSTYAAVSVF TTFGDLAKVP WAKEAIDAMA SRGVIKGTGE NTFSPAASIK
RADFIALLVR ALELHGTGTT DTAMFSDVPA NAYYYNELAV AKQLGIATGF EDNTFKPDSS
ISRQDMMVLT TRALAVLGKQ LPAGGSLNAF SDAASVAGYA QDSVAALVKA GVVQGSGSKL
APNDQLTRAE AAVILYRIWK LQ
