ID M0FBM5_9EURY Unreviewed; 344 AA.
AC M0FBM5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Pectin methylesterase {ECO:0000313|EMBL:ELZ56617.1};
GN ORFNames=C460_13479 {ECO:0000313|EMBL:ELZ56617.1};
OS Haloferax sp. ATCC BAA-646.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=1227464 {ECO:0000313|EMBL:ELZ56617.1, ECO:0000313|Proteomes:UP000011677};
RN [1] {ECO:0000313|Proteomes:UP000011677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-646 {ECO:0000313|Proteomes:UP000011677};
RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA Eisen J.A., Facciotti M.T.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ELZ56617.1, ECO:0000313|Proteomes:UP000011677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-646 {ECO:0000313|EMBL:ELZ56617.1,
RC ECO:0000313|Proteomes:UP000011677};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- SIMILARITY: Belongs to the pectinesterase family.
CC {ECO:0000256|ARBA:ARBA00008891}.
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:ELZ56617.1}.
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DR EMBL; AOLD01000039; ELZ56617.1; -; Genomic_DNA.
DR AlphaFoldDB; M0FBM5; -.
DR PATRIC; fig|1227464.4.peg.2674; -.
DR Proteomes; UP000011677; Unassembled WGS sequence.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IEA:InterPro.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000070; Pectinesterase_cat.
DR PANTHER; PTHR31321; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR PANTHER; PTHR31321:SF141; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 3: Inferred from homology;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023085}.
FT DOMAIN 48..331
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT REGION 21..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 344 AA; 37276 MW; DA68D2E725408D4A CRC64;
MALAVAVGCL AVAAGTVGTL GNADGADDGD ESDDPGDALN SDDPGAYDYV VAKDGSGDYE
TIQAAIDGAK SFPPERIRIL VRDGVYDEKV EVHAWNPDIT LVGESADGTV LTHGDHFERI
GRGRNSTFFT YTLKVRGNDF RARDLTVENS AGPVGQAVSL HVDADRASFE NCRVLGHQDT
VYAAGEGARQ FFSDCYLEGT TDFIFGGATA VFEDCRVHSK ADSYVTAAST PASEPFGFVF
LDCELTADAD VSEVYLGRPW RNHARTAFIR TRMDSHVLPD GWHNWSRPDA EATVEYAEYD
SRGPGASGER VSWATALTED EAERYSKANV LGSVSRGEWW DREE
//