ID A0A402DV15_9CELL Unreviewed; 1468 AA.
AC A0A402DV15;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN ORFNames=CBZ_30230 {ECO:0000313|EMBL:GCE77967.1};
OS Cellulomonas biazotea.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1709 {ECO:0000313|EMBL:GCE77967.1, ECO:0000313|Proteomes:UP000289954};
RN [1] {ECO:0000313|EMBL:GCE77967.1, ECO:0000313|Proteomes:UP000289954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC12680 {ECO:0000313|EMBL:GCE77967.1,
RC ECO:0000313|Proteomes:UP000289954};
RA Yamamura H., Hayashi T., Hamada M., Serisawa Y., Matsuyama K., Nakagawa Y.,
RA Otoguro M., Yanagida F., Hayakawa M.;
RT "Draft genome sequence of Cellulomonas takizawaensis strain TKZ-21.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004115}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
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:GCE77967.1}.
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DR EMBL; BIMR01000281; GCE77967.1; -; Genomic_DNA.
DR OrthoDB; 3771655at2; -.
DR Proteomes; UP000289954; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR CDD; cd00102; IPT; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 5.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR032109; Big_3_5.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR PANTHER; PTHR23303; CARBOXYPEPTIDASE REGULATORY REGION-CONTAINING; 1.
DR PANTHER; PTHR23303:SF14; NODAL MODULATOR 1-RELATED; 1.
DR Pfam; PF16640; Big_3_5; 1.
DR Pfam; PF13620; CarboxypepD_reg; 4.
DR Pfam; PF01833; TIG; 2.
DR SMART; SM00429; IPT; 2.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 3.
DR SUPFAM; SSF81296; E set domains; 2.
DR SUPFAM; SSF49452; Starch-binding domain-like; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..1468
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039517435"
FT DOMAIN 835..917
FT /note="IPT/TIG"
FT /evidence="ECO:0000259|SMART:SM00429"
FT DOMAIN 1013..1095
FT /note="IPT/TIG"
FT /evidence="ECO:0000259|SMART:SM00429"
SQ SEQUENCE 1468 AA; 144783 MW; 079C10A6B797AAF9 CRC64;
MSLVPAPARS RRRRPLGRAM VAAGVAAVVV AGAVAPAAAE PATGTIAGTV TTPAGVSPTF
VTVLVLDPDG GGAGGGSAPV GTDGTYRVED VPAGDWALLF ATGDSDLIPE YFDDAALLAT
STTVAVAGGG TATADATLEL GGVIEGTVRD GAGNPVAGAF VNASRSDWSS GGAYDTTDDE
GRYHLGGLRS GGYRILANPL GGSSLLLGWV GGGTSQQTAA VIAAQQGVTV VGQDAVLPTA
GMAAGRLRSA TGAVVGGTVQ FTSVTDAGNV VTVTTGADGE FEGRMAPGQY RIRFSGPADS
ALAPQYWGGT ADVSGSVAIS VGAGATFPLG NVVLASGGSI TGTVTDDDGE PVAGVTVTAR
SGLVQRTGVT GADGSYTVAG LATGAYTVSF TPPAGSVLRA EHYDDAAASW EADVVAVTTG
ATTAGIDAEL AVGGGIEGRV LAPGGAPLAG ASVHVWPRDP GTGSAPTPAT TGADGTYHVG
GLAAGAWVVE VVPPFGSTLA REFYLDATTS TAATAVDVTV RETEQLEDVV LEPGASVSGV
VLDPDGAPVA GAWVGAQRAG ASTALSAQTG ADGSYTIIGL PAGGYRVRVS PPWTSTDLVA
VYHPGVAAYE QAQEVTVAVG ASRTLPATRL LRAGVVSGTI TRPDGTPVAG ASVNAYSGTQ
GGSATTAADG TYTIGRLSAD DFRVSVSSSA TMLGTYDGVT TYHDGRTGTQ RRSLATTVSV
VAGQTSGEVD LVVPPRGQTA PDVTVTLDPA TPRIGRPVTA TVQVDGPHGP AVGGVAQLSL
GDDLGDVVLG ADGRGALTFD AFAPEYGLLF AWFTGTAAYD EGQGTVEFLA VEDTTPQVTV
VAPAAGSSVG GTVVTVTGSG FTPSSTVTFG GVPAASVVVD SATSLRATTP TLPAGPAPVV
VTTAGGASAA DVAFTATPEP TTTVLALPAR TVLEGAPVTV TATVSAAAGV PSGNVTFAVN
DALTVVPVVA GVATLRLDGL APGTYGVRAV YAGGGGYASS ATWRYLDVIE RVAPVVSQVT
PAAVSAAGGQ RVKVRGTHLT GATGVSFGGV PGSRVTVVDD GLLEVDVPAH PAGTVPVVVT
TPAGSSAPSG AVQFVDTSAG VVSQVPVRIE DELHVGDQPR CLQVAGTTGV PAGASGVTLN
VTVVAPYEVG YVTVYPDVAG PREATSTVNF EVGQEVANAA FVALPANGRV CYRPVGGIAR
VLLDVTGFTM PDSGTELQDP VRLLDTRPAP FRVGDVDGPV GPRSVHTVQV RGRAGVPADA
TAVIVNATVT NVTGPGNLRL FPAGAAVPNA SVLNYAPGKD KANAAIVALS SSGRLSIFSD
TDGASVDVVL DVTGYVTGDG AYRGVTPSRA LDTRPGAGHV GDLTGPLPAR TPSTFTLPSA
AVPAGATSVV LNVTAIGPNG PGNLRVYPSG QSGVPYASTI NYIPGRDIPN LVVVDLPDSG
PATVTLYSDM EPGGTVHVAA DVAGFVVP
//
