ID A0A2M8WVT1_9MICO Unreviewed; 1837 AA.
AC A0A2M8WVT1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Glycosyl hydrolase family 43 {ECO:0000313|EMBL:PJI95035.1};
GN ORFNames=CLV34_0888 {ECO:0000313|EMBL:PJI95035.1};
OS Luteimicrobium subarcticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Luteimicrobium.
OX NCBI_TaxID=620910 {ECO:0000313|EMBL:PJI95035.1, ECO:0000313|Proteomes:UP000231586};
RN [1] {ECO:0000313|EMBL:PJI95035.1, ECO:0000313|Proteomes:UP000231586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22413 {ECO:0000313|EMBL:PJI95035.1,
RC ECO:0000313|Proteomes:UP000231586};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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:PJI95035.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PGTZ01000006; PJI95035.1; -; Genomic_DNA.
DR OrthoDB; 9758923at2; -.
DR Proteomes; UP000231586; 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; cd08983; GH43_Bt3655-like; 1.
DR CDD; cd09004; GH43_bXyl-like; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.40.2340; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR046780; aBig_2.
DR InterPro; IPR032109; Big_3_5.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF20578; aBig_2; 2.
DR Pfam; PF16640; Big_3_5; 1.
DR Pfam; PF04616; Glyco_hydro_43; 2.
DR Pfam; PF13385; Laminin_G_3; 2.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PJI95035.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000231586};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1837
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014643911"
FT DOMAIN 277..357
FT /note="Atrophied bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF20578"
FT DOMAIN 365..446
FT /note="Atrophied bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF20578"
FT DOMAIN 1647..1731
FT /note="Bacterial Ig-like"
FT /evidence="ECO:0000259|Pfam:PF16640"
FT ACT_SITE 1178
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 1339
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 1291
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 1837 AA; 189494 MW; 1BFC6CE6A600FA27 CRC64;
MRNTRRATAV GTAAVLAATM LPSVSAHAAG RAADDVTADV SAADLSSGLI AYYPLDETSG
TTAHDASGNG KDATVEGTAT WNAGDGFTFG GGSAGSGNAI KLPNNLVAGK DDVTVDFDVY
VDASLTGSWF MYNLGNSATY PNGTGYFFTT GAGGTLRGTL ATAGYSTEQS VKKSGALATG
TWKHVTYVLD GGTTAAPGSA QLYEDGALVG SSTAITQSPA QIGEPDGTST RNYLGRSGYP
ADASFKGKIR DFRVYGRTLD AAEAAALAED TAEAGADAAL SALDLGDLSA VTDDLALPKS
AQGATVTWTS STPTVIATDG TVTRPAAGQP SATVTLTASV TNGTATRTKA FTATVLAAPA
SSDKVAYDAE HLTVTNLDDV RGNLTLPTDG HYGSAITWAS PAADVVSATG EVTRPAYGED
AVDVALTATA TLGDDHATRT YTAHVQPLPR TVPTTRYMYS YFTGDSLPGE KIYFAASQGN
DALKWSELND GEPVLTSTLG TKGLRDPFIM RSHDGDTFYL IATDLSIGSG TSWGDSVRTG
SKNIEIWEST DLVHWSDQRQ VKVSPDTAGN TWAPEAYWDD EIGSYVVFWA SSLYDPTDTA
HSGSTYHRMM YATTRDFVTF SPAKVWQDSG KSRIDTTVYK EGDTYYRFTK DEASAGGCTD
IFQDESTDLL APVADWTVQD TCIATKAGLV RAEGPSIFKA NAGDVNGGGY YLFVDEYGYR
KYLPLHSDSL ANPDWETPAS WSLPSSPRHG TVMNITEGEW DGITGTAASA VTSTTKVTLA
DTVVEQGDAT TATVTVKASD GGQVAGDVVV SAGSWSTTVH LDADDAGKAV VDLPADLPVG
AVEVSAAYAG YGVVGASSGK ATLSVGAPTV DPDLVVSYPL DETSGTVVHD ASGHGLDATL
VNGAVPSASG VTLDGTNDYV DLPDDVLQDL TSTTVSIDVK IDASQTTPYF VYGLGNTDSS
GVGNGYLFTT GDGYRTAIAS GNWTTEQNTT KGSNLARGVW KHLTYTLDAA TKTGTLYEDG
VKVAQNTGVT LTPGSIGNGS TLANYIGRSV YTADTYLKGQ VRDFRIYDRA LSSAEVLAQA
GNTTAVVGAS LDTLKVPAIV DSASSTVTLP VKPGTDLSAL APTLELVPGA TVSPANGSVH
DFSQPVTYTV TGSDGATQAW TVKALVMNSP VLPGYNADPN IVVFGDTYYI YATTDGVAGW
GSTSFTVWSS KNLVDWTDHG VILDLGPDVS WADGHAWAPT ITEKDGRYYF YFVADQQIGV
AVSDSPTGHF TDALGEPLIH KADFGGAQQI DPAVFTDTDG TTYLFWGNGT ARMVPLNEDL
ISYDASKVTT ISGLTDFREG LFVNKRNDTY YLTWSVDDTG SENYHVSYAT ASSVDGPWTN
RGTLLAKDPS QGILGTGHSS IVQVPGTDDW YIAYHRFGIP GGDGTHRETT IDRVTFSPDG
LMNPVVPTLT SVAPEVVPDL TKPTVSWVTS PGAADGSAGW FTTSPVSVTA TGADETALAS
TEISVDGGGF VAGSAATSVT ASLADGRHLV QARATDAAGN VSDVVSLAVL VDSAAPVSSG
TVDADARTVT LRAADGLSGV ARVEYRVGAT GSWSAYSAPV TVGAAATAVQ YRAVDVAGNV
EMTNTATVPE AGVVLRDSVT AAVASSSSAT YGKSVKVTVK VSGTGGIPSG TVRVTEGKTL
VGSAKLVSGR ATVSVSSALA VGPHALVVAY SGDKAFAGSS DTVTVKVAKA SSSTSVSVSP
KAPTHVQRAT VTAKVSTAKP SGTVTVTVTH KVAVKQGKAT TTVTRTVVSS RVALSSNGTA
SLRLPQLAKG TYTVKVAYAG SSTATGSSAT TTLRITK
//
