ID C6M9D2_NEISI Unreviewed; 1436 AA.
AC C6M9D2;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 80.
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 ECO:0000313|EMBL:EET43100.1};
GN ORFNames=NEISICOT_03157 {ECO:0000313|EMBL:EET43100.1};
OS Neisseria sicca ATCC 29256.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=547045 {ECO:0000313|EMBL:EET43100.1, ECO:0000313|Proteomes:UP000005365};
RN [1] {ECO:0000313|EMBL:EET43100.1, ECO:0000313|Proteomes:UP000005365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29256 {ECO:0000313|EMBL:EET43100.1,
RC ECO:0000313|Proteomes:UP000005365};
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., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUL-2009) 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:EET43100.1}.
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DR EMBL; ACKO02000027; EET43100.1; -; Genomic_DNA.
DR RefSeq; WP_003761180.1; NZ_ACKO02000027.1.
DR STRING; 490.A6J88_11485; -.
DR eggNOG; COG0296; Bacteria.
DR eggNOG; COG1640; Bacteria.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000005365; 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; 1.
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 944..1298
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 1102
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685"
FT ACT_SITE 1155
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685"
SQ SEQUENCE 1436 AA; 162928 MW; B78E9CEFB154E105 CRC64;
MSEHLEEQAA GLGIDLGFHD IGGIYHATKP EVLEGIIKAL QQDGFSDDLY ADTLVAHENG
RESLQLPAEF HSAAEVCLED EAGGRQVLPL NHGEDGALWV ALPALACGYY TLSAEAEGGV
RKVRLVVAPQ SVYQPKTLEH GLRMNGLTTH LYSLRSQRNW GIGDFTDLLD LMAFAADKQL
DFVGINPLHA LFSAKPAFAS PYSPSSREWL NPIYLDVEKV GAFTYNEKLK NWLKQPNICQ
RIAALRITET VAYTAVWAFK RDALQRAFDA FENDGCEAAE QERAAFDAFV EERGWALEGF
GLFEALDQYY NRSGEVGWLS WPAEFHDPHG EAVQRFAQGH RREIRFYMWL QWLCAEQLRE
VNEAAAARSV KLGIYGDLAV GVARGSADTW LNRADYCMDM AVGAPPDPFS PTGQNWDLPP
LNPMMLKHTG YEKFVRLLRE NMRLYGILRI DHVMALCRLW WVAGKTADFG AYVHYDADVM
FAILALESRR NRCVVIGEDL GTVPDQARYL LNRYQVFSYK VVYFSKGWHG FELPEEYPEQ
AITVVSTHDV APLAGYWTGK DLDLMFRLGT IPDAETFQTT LEAREHDKAD LFDKLKHAGC
LPADAEMSSE IDETLLTALH RYAAMSRSKL YAVQLENLLG MSDNLNVPGV SEGYPNWARK
MPAALEDFPH NRLMGGQLAM IGEVRMKKNS RMKPYHELDQ VERDTVESLF LATHSDLFAY
LGRHRLAEGD EVVRTLIPNA WGVDIVNRET GELITSSEKV DEHGFFVAVL PEGAPNYALN
VRYAEDAEPV REEDPYRFGS ALKDMDSWLL AEGKHLRPYE ALGAHFAEVD GVKGVSFAVW
APNAQRVSVI GEFNHWDGRR HVMRFHRDNG IWDIFIPAVK LNALYKFEIR DANGNVRQKT
DPYAFGAELR PNTASVVRGL PEKVETPDFR ARANAIDAPI SIYEVHLGSW KRNPENNFWL
TYEQLAKELV AYVKDMGFTH IEFLPVSEYP FDGSWGYQAT GLYAPTSRFG SPDELRALIK
AAHDEGIGVI LDWVVGHFPT DDHGLAKFDG TALYEHADPR EGYHQDWNTL IYNFGRNEVK
NFLQGNALYW IERFGFDGIR VDAVASMIYR NYSRKDGEWI PNQYGGHENL EAIAFLRDTN
TMLKEVVPSA TEIAEESTSF ANVTRQEGLN FSYKWNMGWM NDTLRYMMED PINRKYHHNK
MTFGMMYQYS ENFVLPLSHD EVVHGKRSLL GRMPGDCWQQ FANLRAYYGF MYGFPGKKLL
FMGNEFAQGR EWNYNEGLDW FLLDQEGGWH KGVQNFVRDL NRVYKDTAPL YQLDQWPEGF
EWLVADDGNN SVFVFERRNR EGNRVIVISN FTPVVHDSYR FGVNEAGEYR EILNSDDPGY
NGSGVSAGQI LQTEEIWSHG RPNSLAVKVP PLATVYLYKA AEPRATEAAE QAEGEA
//
