ID   Q2Y966_NITMU            Unreviewed;      1730 AA.
AC   Q2Y966;
DT   20-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=4-alpha-glucanotransferase {ECO:0000256|ARBA:ARBA00020295, ECO:0000256|RuleBase:RU361207};
DE            EC=2.4.1.25 {ECO:0000256|ARBA:ARBA00012560, ECO:0000256|RuleBase:RU361207};
DE   AltName: Full=Amylomaltase {ECO:0000256|ARBA:ARBA00031423, ECO:0000256|RuleBase:RU361207};
DE   AltName: Full=Disproportionating enzyme {ECO:0000256|ARBA:ARBA00031501, ECO:0000256|RuleBase:RU361207};
GN   OrderedLocusNames=Nmul_A1402 {ECO:0000313|EMBL:ABB74705.1};
GN   ORFNames=SAMN05216403_10786 {ECO:0000313|EMBL:SEF73637.1};
OS   Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=323848 {ECO:0000313|EMBL:ABB74705.1, ECO:0000313|Proteomes:UP000002718};
RN   [1] {ECO:0000313|EMBL:ABB74705.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 25196 {ECO:0000313|EMBL:ABB74705.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of Chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 / NCIMB 11849 / C 71
RC   {ECO:0000313|Proteomes:UP000002718};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ABB74705.1, ECO:0000313|Proteomes:UP000002718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 {ECO:0000313|EMBL:ABB74705.1}, and ATCC 25196 /
RC   NCIMB 11849 / C 71 {ECO:0000313|Proteomes:UP000002718};
RX   PubMed=18390676; DOI=10.1128/AEM.02722-07;
RA   Norton J.M., Klotz M.G., Stein L.Y., Arp D.J., Bottomley P.J., Chain P.S.,
RA   Hauser L.J., Land M.L., Larimer F.W., Shin M.W., Starkenburg S.R.;
RT   "Complete genome sequence of Nitrosospira multiformis, an ammonia-oxidizing
RT   bacterium from the soil environment.";
RL   Appl. Environ. Microbiol. 74:3559-3572(2008).
RN   [4] {ECO:0000313|EMBL:SEF73637.1, ECO:0000313|Proteomes:UP000236751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nl13 {ECO:0000313|EMBL:SEF73637.1,
RC   ECO:0000313|Proteomes:UP000236751};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC       {ECO:0000256|ARBA:ARBA00005684, ECO:0000256|RuleBase:RU361207}.
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DR   EMBL; CP000103; ABB74705.1; -; Genomic_DNA.
DR   EMBL; FNVK01000007; SEF73637.1; -; Genomic_DNA.
DR   RefSeq; WP_011380741.1; NZ_FNVK01000007.1.
DR   STRING; 323848.Nmul_A1402; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   CAZy; GH77; Glycoside Hydrolase Family 77.
DR   KEGG; nmu:Nmul_A1402; -.
DR   eggNOG; COG1640; Bacteria.
DR   eggNOG; COG3280; Bacteria.
DR   HOGENOM; CLU_002501_0_1_4; -.
DR   OrthoDB; 9761577at2; -.
DR   Proteomes; UP000002718; Chromosome.
DR   Proteomes; UP000236751; Unassembled WGS sequence.
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:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11336; AmyAc_MTSase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 5.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR003385; Glyco_hydro_77.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR012767; Trehalose_TreY.
DR   NCBIfam; TIGR00217; malQ; 1.
DR   NCBIfam; TIGR02401; trehalose_TreY; 1.
DR   PANTHER; PTHR32438; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC/AMYLOPLASTIC; 1.
DR   PANTHER; PTHR32438:SF5; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02446; Glyco_hydro_77; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 2.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361207};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU361207};
KW   Isomerase {ECO:0000313|EMBL:ABB74705.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002718};
KW   Transferase {ECO:0000256|RuleBase:RU361207}.
FT   DOMAIN          765..1573
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1730 AA;  197105 MW;  4DF352A5A50581A5 CRC64;
     MSNPLDQLCE LYGVLPCYSD IWGNTRYTSQ DAKRALLGAM GVAAATEEEI SASLHIFIRR
     KWEHVLPPVQ VVREWMRPYR IAVALPALEG KGRYRWRLCR ESGTEDHDEF IPDALEEVER
     YRFTAPGNFG SFDDPGEQEF VRRILVLDLS VEPGYHRLFI EKSDGLALAE MPFIMAPATC
     YWPPGLEGPR RVWGPALQLY GIRSQRNYGI GDFSDLRRLV EFYASAGGST LLLNPLHALF
     PDAPEHTSPY SPSSRTWFNP LYLDVEAIPE FAECEEARSI VLAPEFQARL RALRATEQVD
     YRGVAEAKSE VLVSLYRYFR NTHLARNTDR ARVFRAFQAE HGEVLRKQAL FEALQEYFRA
     EDSSVWGWRV WPEAYRDPEA PEVTAFREAH LERVEYFEYL QWQVSLQLGS VGTRSWEVGL
     NIGLMFDLAI GVAEGGGATW SRRELYALEA SAGAPPDDFN RLGQNWGLPP WIPHQLTSSA
     YAPFIEVLRA NMRDSGSLRI DHVMGLRRLF WVVRGLPATE GAYIRYPFED MLSILALESQ
     RNRCLVIGED LGTVPPEVRE ALHPANVMST RLLYFERVDG GRLKPPQAYP ANAVVAVTTH
     DLPTLAGFWQ GLDIDLRDRH HLFPEDEMRN RQIVERAADR AQLLVALEGE GVLPSRGGLH
     QVGFPEMTAE LAAAVYTYLA RAPSKLLLLQ LEDGFGVLEQ PNLPGATGDT YPSWRLKLPL
     NLEEWQGSAW LQGIILALRR ERPLSQAPSS SEGEVAQDVQ VQIPRATYRL QLNRDFNLRQ
     ATELIPYLDE LGISHCYLSP LLKARPGSIH GYDVTDHGRL NPEITSARDF ERFAAVLKRH
     GMSQIMDVVP NHMCITGVDN EWWLDVLENG PASRFASYFD IDWYVMGEHL PGQVLLPVLG
     DHYGTVLENG ELKLAFDIEQ GSFSVFYHEH RFPVDPREYP RILGHDLRRL EMRLGEQHPE
     FLELQSLITA LTHLPLRERV SPDAVAERVR DKEIHKRHLA SLFVKSADIA QFVQENITLF
     NGDAPGQPRN FDLLHELLAV QAYRLAFWRA AADEINYRRF FDINDLAALR MDNPEVFEST
     HRLVRELIAR GYVSGLRIDH PDGLYAPQEY FERLQAMAAA ALFPGTVKDG AKSLYIVAEK
     ILASYEHLPK AWSIHGTTGY DFAAACTGLF VDTHAAGEFT RIYERFIRAR PDLDAMIRAN
     KHLIMDRALA GELQVLAIQL ARIAKGDRRT CDFTFNSQHS ALAQVVANFP VYRTYVSDCE
     SSADDVRYAD WAVEVAKKRS QAVDTTIFDF VRDVLLGRQA KGQAEAYRNA ICTFAMKFQQ
     YTSPVMAKAM EDTTFYQYNR LVSLNEVGNE PQRFGVSLAA FHRENQERAS HWPHAMLSTS
     SHDSKRSEDV RARISVLSEI PDQWAQALKR WNRLNRSSRW ELDNTYAPSR NDEYLLYQIL
     LGIWPFDTPH AEELANLSDR VVAYMRKAAR EAKVNSSWIN PDSEYEAAMQ DFVHALLSEQ
     PTNLFLRDFL PFQQRVAWVG AFNSLSQVLL KLTSPGVPDI YQGNETWDFS LVDPDNRRPV
     DYTARRRSLQ AIRSMHAEEG PGACAQHLME NLRDGRIKLY LTWKALTFRR EHEQLFRDGD
     YLPLKAHGDC SEHVCVFARR RENEIIVVAV PRLLGKLIGE QHRFPVGKSI WTDTWVELPS
     DELREKWINV LTGEILATQR TEEACGKFGL AHLFGTFPYA LLSPFEQTTG
//