ID I3R5J6_HALMT Unreviewed; 707 AA.
AC I3R5J6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 2.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Glucan 1,4-alpha-maltohydrolase /alpha-glucosidase {ECO:0000313|EMBL:AFK19506.2};
GN Name=amy4 {ECO:0000313|EMBL:AFK19506.2};
GN OrderedLocusNames=HFX_1802 {ECO:0000313|EMBL:AFK19506.2};
OS Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=523841 {ECO:0000313|EMBL:AFK19506.2, ECO:0000313|Proteomes:UP000006469};
RN [1] {ECO:0000313|EMBL:AFK19506.2, ECO:0000313|Proteomes:UP000006469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC R-4 {ECO:0000313|Proteomes:UP000006469};
RX PubMed=22843593; DOI=10.1128/JB.00880-12;
RA Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA Zhou J., Hu S., Xiang H.;
RT "Complete genome sequence of the metabolically versatile halophilic
RT archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT hydroxyvalerate) producer.";
RL J. Bacteriol. 194:4463-4464(2012).
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DR EMBL; CP001868; AFK19506.2; -; Genomic_DNA.
DR AlphaFoldDB; I3R5J6; -.
DR SMR; I3R5J6; -.
DR STRING; 523841.HFX_1802; -.
DR KEGG; hme:HFX_1802; -.
DR eggNOG; arCOG02948; Archaea.
DR HOGENOM; CLU_024673_0_0_2; -.
DR Proteomes; UP000006469; Chromosome.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11313; AmyAc_arch_bac_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR022567; DUF3459.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR NCBIfam; NF041321; Alpha-amyl_MalA_Halo; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR Pfam; PF00128; Alpha-amylase; 2.
DR Pfam; PF11941; DUF3459; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 4: Predicted;
FT DOMAIN 288..623
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 707 AA; 78236 MW; FD5783EC1B550C15 CRC64;
MHHPGPPQFM AVGESVQLAP RNPNPDADYE WHVRSAPVAS SLDFEEGTPV VQFTPDAEGS
YVLELDAPDG PHTLTVRVFP GSYLPSGSVR SGESGMSGFS GFSGQSGSAR PTQFSGGASG
SGSGAGEAQR GDGGRPRIRL DATVEDGVVV VRADPQPNPN SDTDRDDLVV EFVVDDRDDV
NRSAVETDGW ELRIPVSAIG DRLRVHGVAL DETYSVPDTV TVERDAITDG GVAEAEHEGE
AEHEGATTEG ETNDTESTAK SDGSGGQRVS VARPNDPPKW AQEVTLYEIY VRGYTSGVDE
KGSSDRQTQS GDVGDDEVEN TFEALENRLD YLESLGVDCL WLTPVLQNDH APHGYNIVDF
YSIAEDLGSR EDYEQFVEAA HDRGMKVLFD LVLNHSAREH PFFKDAYKNP DSDYYDWYEW
QENGEPGTYF DWEYIANFDH RNLDVRRYLL DAVDMWAEIV DGFRCDMAWA VPDTFWQEIR
DRVKSKDSDF LLLDETIPYI ADFHEGMFDM HFDTTLYFVL RQVGRGDAPA ERILDAIDQR
AEVGFPDHAA FMLYLENHDE TRYIVECGES EALAGAGALF TLPGVPMIYG GQEIGQRGRR
DALSWEHARD DIREHYERLI EVRDETPALR YGGSFRRIDY ETDSDRAVAF VRDHADGSYL
CLLHFGDGSV TVDIGDLDVD ATDLVSGDSI AAEGGLRVDD VAICPLV
//