ID A0A1R3KQN7_9ROSI Unreviewed; 762 AA.
AC A0A1R3KQN7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 13-SEP-2023, entry version 23.
DE SubName: Full=Pectinesterase, catalytic {ECO:0000313|EMBL:OMP09374.1};
GN ORFNames=COLO4_05544 {ECO:0000313|EMBL:OMP09374.1};
OS Corchorus olitorius.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=93759 {ECO:0000313|EMBL:OMP09374.1, ECO:0000313|Proteomes:UP000187203};
RN [1] {ECO:0000313|Proteomes:UP000187203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. O-4 {ECO:0000313|Proteomes:UP000187203};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M., Yahiya A.S., Khan M.S.,
RA Azam M.S., Haque T., Lashkar M.Z.H., Akhand A.I., Morshed G., Roy S.,
RA Uddin K.S., Rabeya T., Hossain A.S., Chowdhury A., Snigdha A.R.,
RA Mortoza M.S., Matin S.A., Hoque S.M.E., Islam M.K., Roy D.K., Haider R.,
RA Moosa M.M., Elias S.M., Hasan A.M., Jahan S., Shafiuddin M., Mahmood N.,
RA Shommy N.S.;
RT "Corchorus olitorius genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5. {ECO:0000256|ARBA:ARBA00005184}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ferroportin (FP) (TC 2.A.100) family. SLC40A
CC subfamily. {ECO:0000256|ARBA:ARBA00006279}.
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:OMP09374.1}.
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DR EMBL; AWUE01012367; OMP09374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3KQN7; -.
DR STRING; 93759.A0A1R3KQN7; -.
DR OrthoDB; 897443at2759; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000187203; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd17480; MFS_SLC40A1_like; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR009716; Ferroportin-1.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000070; Pectinesterase_cat.
DR PANTHER; PTHR11660; SOLUTE CARRIER FAMILY 40 MEMBER; 1.
DR PANTHER; PTHR11660:SF53; SOLUTE CARRIER FAMILY 40 MEMBER 3, CHLOROPLASTIC; 1.
DR Pfam; PF06963; FPN1; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000187203};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 344..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..436
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 457..479
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 491..510
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 559..576
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 596..615
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 622..645
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 657..678
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 690..715
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 721..743
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..177
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
SQ SEQUENCE 762 AA; 82505 MW; F59F4C2E201B7092 CRC64;
METFKRFNLQ SIPSLQTIID GSNFKSNLVS TTDNIVAKGI TFKAIAATIF GDKSAFFGCR
FLGLQDTLYS ARGRHYFSSC YIEGGADFIF GNGQSFFEDC SINVTAGAFA PQMRLGYITA
QGRDSPNDPS GFVFEGGKIF GTLKHYLGRA WGPYSRVIFH HTILSAEVVP LRWFAWNYPG
KEREASLSRQ AASRIRYRFS SSRWLNLNLN SPYTFPPHPH HSFKSRCSIT DVQFSHVTTE
NEVPEDISGT EIACCCATAT PIVQLKPDIL ETEPLSILTG DTYVDSLLTT LPVLSEEEQK
ALAATPAHPE GLYAFYASCL AGNLVEQLWN FAWPSAIALL HPSLLPVAVM GFFTKLVIIV
GGPLVGKLMD NSPRVPSHIF LNVVQAAAQL LSAAMIIHAH TVSPASASSV LLRPWFAVLV
LAGAVERLSG VALGVAMERD WVVLLAGINR PIALAQANAV LNRIDLLCEI AGASLFGILL
SKYDPVTCLK FAAGLMMWSL PVMISLTWLT NKLSTGVLDR AKCSQIGCFD DGPLPDAANF
VNTGLEAIKL GWREYIQQPV LPASLAYVLL YFNVVLTPGS LMTAFLTQRG LNPSVIGGFS
GLCAFMGVAA TFLSATLVRR FGILKAGAVG LICQASLLIA AVAVYNSGSL TQKSPLLFFL
SLIVLSRLGH MSYDLIGAQI LQTGIPSSKA NLIGTTEISV ASLAESLMLG VVIIANDVSH
FGFLAMLSLL SVVGAAWMFC RWLSNITEEQ RSLFSFDPQF QL
//
