(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 125.
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;
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}.
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   SMR; P42404; -.
DR   STRING; 224308.BSU03450; -.
DR   PaxDb; P42404; -.
DR   PRIDE; P42404; -.
DR   EnsemblBacteria; CAB12139; CAB12139; BSU03450.
DR   GeneID; 938313; -.
DR   KEGG; bsu:BSU03450; -.
DR   PATRIC; fig|224308.179.peg.362; -.
DR   eggNOG; ENOG41080HJ; Bacteria.
DR   eggNOG; COG0794; LUCA.
DR   HOGENOM; HOG000251683; -.
DR   InParanoid; P42404; -.
DR   KO; K08094; -.
DR   OMA; IQPMGSL; -.
DR   PhylomeDB; P42404; -.
DR   BioCyc; BSUB:BSU03450-MONOMER; -.
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.
DR   PANTHER; PTHR43443; PTHR43443; 1.
DR   Pfam; PF01380; SIS; 1.
DR   TIGRFAMs; TIGR03127; RuMP_HxlB; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P42404.
DR   SWISS-2DPAGE; P42404.
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   REGION          86..91
FT                   /note="Substrate-binding"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305"
FT   BINDING         47
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255"
FT   HELIX           3..18
FT                   /evidence="ECO:0000244|PDB:1M3S"
FT   HELIX           23..35
FT                   /evidence="ECO:0000244|PDB:1M3S"
FT   STRAND          39..42
FT                   /evidence="ECO:0000244|PDB:1M3S"
FT   HELIX           45..60
FT                   /evidence="ECO:0000244|PDB:1M3S"
FT   STRAND          65..67
FT                   /evidence="ECO:0000244|PDB:1M3S"
FT   STRAND          81..85
FT                   /evidence="ECO:0000244|PDB:1M3S"
FT   STRAND          87..89
FT                   /evidence="ECO:0000244|PDB:1M3S"
FT   HELIX           92..103
FT                   /evidence="ECO:0000244|PDB:1M3S"
FT   STRAND          107..113
FT                   /evidence="ECO:0000244|PDB:1M3S"
FT   HELIX           118..122
FT                   /evidence="ECO:0000244|PDB:1M3S"
FT   STRAND          124..128
FT                   /evidence="ECO:0000244|PDB:1M3S"
FT   HELIX           133..137
FT                   /evidence="ECO:0000244|PDB:1VIV"
FT   HELIX           149..169
FT                   /evidence="ECO:0000244|PDB:1M3S"
FT   TURN            174..176
FT                   /evidence="ECO:0000244|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
//

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