ID K6C280_9BACI Unreviewed; 388 AA.
AC K6C280;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Tagatose-6-phosphate ketose/aldose isomerase {ECO:0000313|EMBL:EKN65255.1};
GN ORFNames=BABA_21461 {ECO:0000313|EMBL:EKN65255.1};
OS Neobacillus bataviensis LMG 21833.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN65255.1, ECO:0000313|Proteomes:UP000006316};
RN [1] {ECO:0000313|EMBL:EKN65255.1, ECO:0000313|Proteomes:UP000006316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX PubMed=23087684;
RA Heylen K., Keltjens J.;
RT "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT reduction in Bacillus.";
RL Front. Microbiol. 3:371-371(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactosamine 6-phosphate + H2O = D-tagatopyranose 1-
CC phosphate + NH4(+); Xref=Rhea:RHEA:47680, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:71674, ChEBI:CHEBI:138150;
CC Evidence={ECO:0000256|ARBA:ARBA00029292};
CC -!- SIMILARITY: Belongs to the SIS family. AgaS subfamily.
CC {ECO:0000256|ARBA:ARBA00007748}.
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:EKN65255.1}.
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DR EMBL; AJLS01000137; EKN65255.1; -; Genomic_DNA.
DR RefSeq; WP_007087284.1; NZ_AJLS01000137.1.
DR AlphaFoldDB; K6C280; -.
DR STRING; 1117379.BABA_21461; -.
DR PATRIC; fig|1117379.3.peg.4449; -.
DR eggNOG; COG2222; Bacteria.
DR OrthoDB; 9779207at2; -.
DR Proteomes; UP000006316; Unassembled WGS sequence.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR CDD; cd05010; SIS_AgaS_like; 1.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035464; SIS_AgaS.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR PANTHER; PTHR32502:SF3; D-GALACTOSAMINE-6-PHOSPHATE DEAMINASE AGAS-RELATED; 1.
DR PANTHER; PTHR32502; N-ACETYLGALACTOSAMINE PERMEASE II COMPONENT-RELATED; 1.
DR Pfam; PF01380; SIS; 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51464; SIS; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Isomerase {ECO:0000313|EMBL:EKN65255.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006316};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 42..202
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 221..369
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 388 AA; 42277 MW; DBB8702DEADFC92B CRC64;
MFTLSPEKLM PLGAAITTAE IKQQPELWGE AFALYTGKSQ KIESFLQNIT EKHNRVRVIF
TGAGTSAYVG DTITPYLKEK VDENQWDLMS VSTTAIVSNP YQFLKADIPT LLISFARSGN
SPESVATVEL AEQVVKDLYQ ITITCSKEGK LAQRAKGDDS NLLLLMPEKS NDQGFAMTGS
YTCMALTALL IFDSLSVEEK SSIVANIRKM GQTVINKEAA IEQMIADGFE RIIYLGSGGF
EGLAREAQLK ILELTAGKIA TSFDSSLGFR HGPKSFVNEK TAIFVFVSNQ PYTRQYDLDM
LQELSQDQIA STICAISVVG ETNFAGDTFS FDGSAARVPD AYLSLPYVMV GQTIALFASI
KVGNTPDTPS PSGTVNRVVK GVTIHEYK
//
