ID G9ZGX1_9GAMM Unreviewed; 1498 AA.
AC G9ZGX1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000256|HAMAP-Rule:MF_00685};
DE EC=2.4.1.18 {ECO:0000256|HAMAP-Rule:MF_00685};
DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000256|HAMAP-Rule:MF_00685};
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685};
DE AltName: Full=Glycogen branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685};
DE Short=BE {ECO:0000256|HAMAP-Rule:MF_00685};
GN Name=glgB {ECO:0000256|HAMAP-Rule:MF_00685};
GN ORFNames=HMPREF9080_02028 {ECO:0000313|EMBL:EHM52995.1};
OS Cardiobacterium valvarum F0432.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC Cardiobacteriaceae; Cardiobacterium.
OX NCBI_TaxID=797473 {ECO:0000313|EMBL:EHM52995.1, ECO:0000313|Proteomes:UP000004750};
RN [1] {ECO:0000313|EMBL:EHM52995.1, ECO:0000313|Proteomes:UP000004750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0432 {ECO:0000313|EMBL:EHM52995.1,
RC ECO:0000313|Proteomes:UP000004750};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages
CC in glycogen by scission of a 1,4-alpha-linked oligosaccharide from
CC growing alpha-1,4-glucan chains and the subsequent attachment of the
CC oligosaccharide to the alpha-1,6 position.
CC {ECO:0000256|ARBA:ARBA00002953, ECO:0000256|HAMAP-Rule:MF_00685}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a
CC primary hydroxy group in a similar glucan chain.; EC=2.4.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00000826, ECO:0000256|HAMAP-
CC Rule:MF_00685};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new
CC position in an acceptor, which may be glucose or a (1->4)-alpha-D-
CC glucan.; EC=2.4.1.25; Evidence={ECO:0000256|ARBA:ARBA00000439,
CC ECO:0000256|RuleBase:RU361207};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004964, ECO:0000256|HAMAP-Rule:MF_00685}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00685}.
CC -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC {ECO:0000256|ARBA:ARBA00005684, ECO:0000256|RuleBase:RU361207}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000256|ARBA:ARBA00009000, ECO:0000256|HAMAP-
CC Rule:MF_00685}.
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:EHM52995.1}.
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DR EMBL; AGCM01000115; EHM52995.1; -; Genomic_DNA.
DR STRING; 797473.HMPREF9080_02028; -.
DR PATRIC; fig|797473.3.peg.1652; -.
DR HOGENOM; CLU_004150_0_0_6; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000004750; Unassembled WGS sequence.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-UniRule.
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:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd11322; AmyAc_Glg_BE; 1.
DR CDD; cd02855; E_set_GBE_prok_N; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR HAMAP; MF_00685; GlgB; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR006407; GlgB.
DR InterPro; IPR044143; GlgB_N_E_set_prok.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004193; Glyco_hydro_13_N.
DR InterPro; IPR003385; Glyco_hydro_77.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR NCBIfam; TIGR01515; branching_enzym; 1.
DR NCBIfam; TIGR00217; malQ; 1.
DR PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR PANTHER; PTHR43651:SF3; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF02446; Glyco_hydro_77; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF81296; E set domains; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00685,
KW ECO:0000256|RuleBase:RU361207};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00685}.
FT DOMAIN 994..1354
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 1152
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685"
FT ACT_SITE 1205
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685"
SQ SEQUENCE 1498 AA; 169905 MW; 793616584A06ED9A CRC64;
MLCVFLLDIA CGCVIFTLCE INTTVREDGQ ERVMNSEQFR LLGIETDYFA ADGSFVRVSD
EVLSSLAAIL TAPGQHLSTS VHFDEVFTVL PEMVALLPIG GLLPRVAAVF LLNEHGQSIP
CSSIMIEGGR IELPPLPSGY YSLELHSAHQ MRRCLLIVAP HSVYQPAALR RGERLSGINV
QLYSLRSQHN WGIGDFGDLR RLVADFTTDG IDFIGINPLH ALFTTHPNWA SPYSPSSRRW
LNPIYLDIND MRLFHISPSA QAWYNEAATQ KQLAELRAAE WVDYAQVLPF KLRALYLVFR
DFCDSDDPIF AAAREAFAKF VEEQGRELRL YGTFEALDHY FYAQNATVPF SEDSVGWLGW
PEAYRYPDSA AVLAFSAAHE ADIRYYMWLQ WLLADQLDNL RHYCGEQGMI LGLYGDLAVG
VSRGGADTWM HRDMYCLQVS VGAPPDEFGP AGQNWGLPPL HPQRLKRSGY QIFINMLRAN
MRYYGVLRID HVMALHRLWW IAYGNSANLG AYVRYPLAEL MAILALESRR ARCVIVGEDL
GIVPDEMRVA LGEYGVYSYG VMYFNHNGAR YLLPEEYPEH ALAVVSTHDL APLAGYWEKN
DLDTMQRLGV FTSDAQYQNL LAQRESRKGQ IIAALHQTEL LGESEDGGKL DDTITLALHR
FVAMSRSRLF AIQPENLLGV TASFNIPGIA NTYPNWRYRL PEDTAAMGKN PQLHDMLRQI
VATRAQPREP LPITAATTAI TTTTGGIEVT SVDKYLIDQL FSGTFADPFS YLGPHENSNG
TALRVLLPGA EAVRVLDHDN PKKVLADMSL LDERGFFIAR LEADVRRYLL QVRYGDKNTV
IIEDPYRFGT TLHDYDNWLL AEGTHLRPYE QFGSHLVEID SVAGVSFSVW APNARRVSVV
GDFNLWDGRR HVMRFHPQSG IWDIFIPGIG EHALYKYEIL DVNGNIRLKS DPYAFGAQLR
PDTASVVTRL PERLPYDPER VTANSIDAPI SIYEVHLGSW RRNPENNFWL SYAQLADELI
PYVKDMGFTH IELLPVAEFP FDGSWGYQPL GLYAPTSRFG TPQELCDFIE KAHDAGIHVL
LDWVVGHFPT DEYGLNRFDG TPLYEHADPR EGYHQDWNTL IYNFGRYEVR NFLTANALYW
IEHYGVDGLR VDAVASMIYR DYSRKEGEWI PNRYGGRENL EAINFLQRTN AILQNEQRGA
VSIAEESTAF TGVSHPTESG GLGFQYKWNM GWMNDTLRYM QEDPVHRKYH HNLLTFGMIY
QYSEHFVLPL SHDEVVHGKG SLLSKMPGDC WQQFANLRAY YGYMWGYPGK KLLFMGGEFA
QGREWNYQES LDWFLLEPQY GGWHEGVQKW VRDLNHVYQE HPALWKQDCN PEGFEWLVVD
DAEQSVIAFA RHGGDGKPVI IVSNFTPVPR ENYRIGVSQA GHYREILNSD STQYNGSGVS
GGEYLHTEDI PSHGRDQSLN LTLPPLGTIF LAYEQIAEAA VQHADNSDKH GKKGNKKR
//
