ID A0A1Z5HBZ9_9GAMM Unreviewed; 554 AA.
AC A0A1Z5HBZ9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=1,4-alpha-glucan branching enzyme {ECO:0000313|EMBL:GAW86820.1};
DE EC=2.4.1.18 {ECO:0000313|EMBL:GAW86820.1};
GN ORFNames=bplSymb_SCF04102P006 {ECO:0000313|EMBL:GAW86820.1};
OS Bathymodiolus platifrons methanotrophic gill symbiont.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=113268 {ECO:0000313|EMBL:GAW86820.1, ECO:0000313|Proteomes:UP000196430};
RN [1] {ECO:0000313|EMBL:GAW86820.1, ECO:0000313|Proteomes:UP000196430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPD1508-B01-01 {ECO:0000313|EMBL:GAW86820.1,
RC ECO:0000313|Proteomes:UP000196430};
RX PubMed=28453654; DOI=10.1093/gbe/evx082;
RA Takishita K., Takaki Y., Chikaraishi Y., Ikuta T., Ozawa G., Yoshida T.,
RA Ohkouchi N., Fujikura K.;
RT "Genomic Evidence that Methanotrophic Endosymbionts Likely Provide Deep-Sea
RT Bathymodiolus Mussels with a Sterol Intermediate in Cholesterol
RT Biosynthesis.";
RL Genome Biol. Evol. 9:1148-1160(2017).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 57 family.
CC {ECO:0000256|ARBA:ARBA00006821, ECO:0000256|RuleBase:RU361196}.
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:GAW86820.1}.
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DR EMBL; BDMN01000221; GAW86820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5HBZ9; -.
DR OrthoDB; 9803279at2; -.
DR Proteomes; UP000196430; Unassembled WGS sequence.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-EC.
DR GO; GO:0102752; F:1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis); IEA:UniProtKB-EC.
DR GO; GO:0030979; P:alpha-glucan biosynthetic process; IEA:InterPro.
DR CDD; cd10792; GH57N_AmyC_like; 1.
DR Gene3D; 1.20.1430.10; Families 57/38 glycoside transferase, middle domain; 1.
DR Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR InterPro; IPR037090; 57_glycoside_trans_central.
DR InterPro; IPR015293; BE_C.
DR InterPro; IPR040042; Branching_enz_MT3115-like.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR004300; Glyco_hydro_57_N.
DR PANTHER; PTHR41695; 1,4-ALPHA-GLUCAN BRANCHING ENZYME RV3031-RELATED; 1.
DR PANTHER; PTHR41695:SF1; 1,4-ALPHA-GLUCAN BRANCHING ENZYME TK1436; 1.
DR Pfam; PF09210; BE_C; 1.
DR Pfam; PF03065; Glyco_hydro_57; 1.
DR SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361196};
KW Glycosyltransferase {ECO:0000313|EMBL:GAW86820.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000196430};
KW Transferase {ECO:0000313|EMBL:GAW86820.1}.
FT DOMAIN 10..395
FT /note="Glycoside hydrolase family 57 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03065"
FT DOMAIN 428..529
FT /note="1,4-alpha-glucan branching enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09210"
FT ACT_SITE 192
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT ACT_SITE 353
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT BINDING 469
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
SQ SEQUENCE 554 AA; 64179 MW; C0E88EFC6ED3B410 CRC64;
MTRKKGFLSI ILHAHLPFVR HPEYDSFFEE IWLFEAITEC YIPLIRSLDR LHKDRINYRL
TLSLSPPLIS MLSDELLQSR YLTYLNSRLE LAEKEILRTK STPEYQKLAR LYRRLYLDTL
DIFAVQYDCN LLTAFKKFHA TGNLELITCA ATHGFLPLLN KSDAAVHNQI HTGVETFISH
LGFNPTGFWL PECGYYPGLE KHLKDAGINY FFVDSHGIEN ASIAPRNSVY APLNCGNDVM
AFARDPESSR QVWSSHEGYP GDHDYREYYS DIGFDLNLDY IAPYILDGDI RINTGIKYHR
VTGTDLPKEI YQPRQALHKA QQHAHDFINK RQLQINRLST DMDRIPIVVS PYDAELFGHW
WYEGPLWLEW VLRFADSTNN SVQTISCSYY LTQIPTHQKA TPSASTWGAQ GYSSFWINET
NDWIYPLLHK AGADMENLAA IFQRVTASPL QERTLNQAVR SLLLAQASDW PFIMQTGTTV
EYAKKRITDH LARFNYLRDS IRNNAIDEDY LSALEILDEV FPDADFRNYY MPEQKPVMNN
KLNYPVGKKV QQQV
//