PHI_BACSU
ID PHI_BACSU Reviewed; 185 AA.
AC P42404;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=3-hexulose-6-phosphate isomerase;
DE EC=5.3.1.27;
DE AltName: Full=6-phospho-3-hexuloisomerase;
DE Short=PHI;
GN Name=hxlB; Synonyms=yckF; OrderedLocusNames=BSU03450;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7704255; DOI=10.1099/13500872-141-2-277;
RA Fujishima Y., Yamane K.;
RT "A 10 kb nucleotide sequence at the 5' flanking region (32 degrees) of
RT srfAA of the Bacillus subtilis chromosome.";
RL Microbiology 141:277-279(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 173-185.
RC STRAIN=168 / OI1085;
RX PubMed=7921238; DOI=10.1099/13500872-140-8-1847;
RA Hanlon D.W., Rosario M.M.L., Ordal G.W., Venema G., van Sinderen D.;
RT "Identification of TlpC, a novel 62 kDa MCP-like protein from Bacillus
RT subtilis.";
RL Microbiology 140:1847-1854(1994).
RN [5]
RP CHARACTERIZATION.
RC STRAIN=168;
RX PubMed=10572115; DOI=10.1128/jb.181.23.7154-7160.1999;
RA Yasueda H., Kawahara Y., Sugimoto S.;
RT "Bacillus subtilis yckG and yckF encode two key enzymes of the ribulose
RT monophosphate pathway used by methylotrophs, and yckH is required for their
RT expression.";
RL J. Bacteriol. 181:7154-7160(1999).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), AND SUBUNIT.
RX PubMed=15363790; DOI=10.1016/j.jsb.2004.04.006;
RA Sanishvili R., Wu R., Kim D.E., Watson J.D., Collart F., Joachimiak A.;
RT "Crystal structure of Bacillus subtilis YckF: structural and functional
RT evolution.";
RL J. Struct. Biol. 148:98-109(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-185.
RX PubMed=16021622; DOI=10.1002/prot.20541;
RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT "Structural analysis of a set of proteins resulting from a bacterial
RT genomics project.";
RL Proteins 60:787-796(2005).
CC -!- FUNCTION: Catalyzes the isomerization between 3-hexulose 6-phosphate
CC and fructose 6-phosphate. Together with HxlA, may act as a formaldehyde
CC detoxification system.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabino-hex-3-ulose 6-phosphate = beta-D-fructose 6-
CC phosphate; Xref=Rhea:RHEA:25900, ChEBI:CHEBI:57634,
CC ChEBI:CHEBI:58542; EC=5.3.1.27;
CC -!- PATHWAY: One-carbon metabolism; formaldehyde assimilation via RuMP
CC pathway; D-fructose 6-phosphate from D-ribulose 5-phosphate and
CC formaldehyde: step 2/2.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15363790}.
CC -!- INDUCTION: By formaldehyde, under the control of HxlR. Not induced by
CC methanol, formate, or methylamine.
CC -!- SIMILARITY: Belongs to the SIS family. PHI subfamily. {ECO:0000305}.
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DR EMBL; D30762; BAA06433.1; -; Genomic_DNA.
DR EMBL; D50453; BAA08979.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12139.1; -; Genomic_DNA.
DR EMBL; Z34005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; H69760; H69760.
DR RefSeq; NP_388227.1; NC_000964.3.
DR RefSeq; WP_003246343.1; NZ_JNCM01000030.1.
DR PDB; 1M3S; X-ray; 1.95 A; A/B=1-185.
DR PDB; 1VIV; X-ray; 2.60 A; A/B=2-185.
DR PDBsum; 1M3S; -.
DR PDBsum; 1VIV; -.
DR AlphaFoldDB; P42404; -.
DR SMR; P42404; -.
DR STRING; 224308.BSU03450; -.
DR PaxDb; P42404; -.
DR PRIDE; P42404; -.
DR EnsemblBacteria; CAB12139; CAB12139; BSU_03450.
DR GeneID; 938313; -.
DR KEGG; bsu:BSU03450; -.
DR PATRIC; fig|224308.179.peg.362; -.
DR eggNOG; COG0794; Bacteria.
DR InParanoid; P42404; -.
DR OMA; KTIQPMG; -.
DR PhylomeDB; P42404; -.
DR BioCyc; BSUB:BSU03450-MON; -.
DR BRENDA; 5.3.1.27; 658.
DR UniPathway; UPA00294; UER00435.
DR EvolutionaryTrace; P42404; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0043800; F:hexulose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019647; P:formaldehyde assimilation via ribulose monophosphate cycle; IEA:UniProtKB-UniPathway.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR CDD; cd05005; SIS_PHI; 1.
DR InterPro; IPR017552; PHI/rmpB.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR PANTHER; PTHR43443; PTHR43443; 1.
DR Pfam; PF01380; SIS; 1.
DR SUPFAM; SSF53697; SSF53697; 1.
DR TIGRFAMs; TIGR03127; RuMP_HxlB; 1.
DR PROSITE; PS51464; SIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Detoxification; Isomerase;
KW Reference proteome.
FT CHAIN 1..185
FT /note="3-hexulose-6-phosphate isomerase"
FT /id="PRO_0000136566"
FT DOMAIN 29..172
FT /note="SIS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 86..91
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:1M3S"
FT HELIX 23..35
FT /evidence="ECO:0007829|PDB:1M3S"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1M3S"
FT HELIX 45..60
FT /evidence="ECO:0007829|PDB:1M3S"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1M3S"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:1M3S"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1M3S"
FT HELIX 92..103
FT /evidence="ECO:0007829|PDB:1M3S"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:1M3S"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:1M3S"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:1M3S"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:1VIV"
FT HELIX 149..169
FT /evidence="ECO:0007829|PDB:1M3S"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:1M3S"
SQ SEQUENCE 185 AA; 19963 MW; 18593390B7CDA79A CRC64;
MKTTEYVAEI LNELHNSAAY ISNEEADQLA DHILSSHQIF TAGAGRSGLM AKSFAMRLMH
MGFNAHIVGE ILTPPLAEGD LVIIGSGSGE TKSLIHTAAK AKSLHGIVAA LTINPESSIG
KQADLIIRMP GSPKDQSNGS YKTIQPMGSL FEQTLLLFYD AVILKLMEKK GLDSETMFTH
HANLE
