ID   G7Z1Q7_AZOL4            Unreviewed;       561 AA.
AC   G7Z1Q7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Putative trehalose synthase {ECO:0000313|EMBL:CBS87190.1};
DE            EC=5.4.99.16 {ECO:0000313|EMBL:CBS87190.1};
GN   OrderedLocusNames=AZOLI_1942 {ECO:0000313|EMBL:CBS87190.1};
OS   Azospirillum lipoferum (strain 4B).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS87190.1, ECO:0000313|Proteomes:UP000005667};
RN   [1] {ECO:0000313|Proteomes:UP000005667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA   Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA   Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA   Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA   Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(2011).
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DR   EMBL; FQ311868; CBS87190.1; -; Genomic_DNA.
DR   RefSeq; WP_014248192.1; NC_016622.1.
DR   AlphaFoldDB; G7Z1Q7; -.
DR   STRING; 862719.AZOLI_1942; -.
DR   KEGG; ali:AZOLI_1942; -.
DR   HOGENOM; CLU_006462_2_3_5; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000005667; Chromosome.
DR   GO; GO:0047471; F:maltose alpha-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11334; AmyAc_TreS; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF219; MALTOSE ALPHA-D-GLUCOSYLTRANSFERASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16657; Malt_amylase_C; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Isomerase {ECO:0000313|EMBL:CBS87190.1}.
FT   DOMAIN          14..415
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   561 AA;  64226 MW;  D52E91C1491DF013 CRC64;
     MIGDLWYKNA VIYNLALSTF MDASGDGIGD FQGLLRRLDY LHGLGVTCIW LGPFQTSPMK
     DDGYDVADYY TVDPRYGTLG DFVEFTHACE QRGIRVIIDL VINHTSDRHP WFKAARSDPG
     SKYRNWYVWS DRKPANADTG MVFPGVQEST WTYDREAKAW YFHRFYKFQP DLNTAHPEVH
     AELLKIMGFW IQLGVAGFRM DAVPFIIAEK GAEVTEPKEQ FGMLRSFREF VQWRRGDAVL
     LAEANILPED DLHYFGDDGD RCHMMFNFQV NQTLFYALAT ADTAPLVTAL KVTKPRPATA
     QWGCFLRNHD ELDLGRLTEE QRQAVFAAFG PEKCMQLYDR GIRRRLAPML HDDRRRIELA
     YSLMFTLPGT PVIRYGDEIG MGDDLSLPER NCARTPMQWS DEPHGGFTKS DGPEIPVIAG
     GVFGYERINA AVQRRDPESL LNWTERIIRM RKECPEIGWG DFQILKTGRP EVLALRYDWR
     NNGVVVLHNL SDKPCEILLD VEGHGEACRL VNLLSEDHSE PDSEGRHDLV LEAYGYRWFR
     VGGLDYLLRR TEADKKPGEG G
//