YITF_BACSU
ID YITF_BACSU Reviewed; 371 AA.
AC O06741; Q796Q2;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Putative isomerase YitF;
DE EC=5.-.-.-;
GN Name=yitF; OrderedLocusNames=BSU10970;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9353932; DOI=10.1099/00221287-143-10-3309;
RA Roche B., Autret S., Levine A., Vannier F., Medina N., Seror S.J.;
RT "A Bacillus subtilis chromosome segment at the 100 degrees to 102 degrees
RT position encoding 11 membrane proteins.";
RL Microbiology 143:3309-3312(1997).
RN [2]
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 [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, AND
RP SUBUNIT.
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of mandelate racemase/muconate lactonizing enzyme from
RT Bacillus subtilis at 1.8 A resolution.";
RL Submitted (APR-2006) to the PDB data bank.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC Note=Divalent metal cations. Mg(2+). {ECO:0000305};
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. {ECO:0000305}.
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DR EMBL; Y09476; CAA70661.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12937.1; -; Genomic_DNA.
DR PIR; G69839; G69839.
DR RefSeq; NP_388978.1; NC_000964.3.
DR RefSeq; WP_003245056.1; NZ_JNCM01000035.1.
DR PDB; 2GDQ; X-ray; 1.80 A; A/B=2-371.
DR PDB; 2GGE; X-ray; 1.89 A; A/B/C/D/E/F/G/H=2-371.
DR PDBsum; 2GDQ; -.
DR PDBsum; 2GGE; -.
DR AlphaFoldDB; O06741; -.
DR SMR; O06741; -.
DR STRING; 224308.BSU10970; -.
DR PaxDb; O06741; -.
DR PRIDE; O06741; -.
DR DNASU; 939345; -.
DR EnsemblBacteria; CAB12937; CAB12937; BSU_10970.
DR GeneID; 939345; -.
DR KEGG; bsu:BSU10970; -.
DR PATRIC; fig|224308.179.peg.1179; -.
DR eggNOG; COG4948; Bacteria.
DR InParanoid; O06741; -.
DR OMA; EYMRHTE; -.
DR PhylomeDB; O06741; -.
DR BioCyc; BSUB:BSU10970-MON; -.
DR EvolutionaryTrace; O06741; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0016052; P:carbohydrate catabolic process; IBA:GO_Central.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..371
FT /note="Putative isomerase YitF"
FT /id="PRO_0000360691"
FT ACT_SITE 158
FT /evidence="ECO:0000250"
FT ACT_SITE 290
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT STRAND 2..21
FT /evidence="ECO:0007829|PDB:2GDQ"
FT STRAND 24..38
FT /evidence="ECO:0007829|PDB:2GDQ"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:2GDQ"
FT HELIX 52..61
FT /evidence="ECO:0007829|PDB:2GDQ"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:2GDQ"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:2GDQ"
FT HELIX 87..104
FT /evidence="ECO:0007829|PDB:2GDQ"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:2GDQ"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:2GDQ"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:2GDQ"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:2GDQ"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:2GDQ"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2GDQ"
FT HELIX 164..178
FT /evidence="ECO:0007829|PDB:2GDQ"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:2GDQ"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:2GDQ"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:2GDQ"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:2GDQ"
FT HELIX 222..229
FT /evidence="ECO:0007829|PDB:2GDQ"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:2GDQ"
FT HELIX 245..253
FT /evidence="ECO:0007829|PDB:2GDQ"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:2GDQ"
FT TURN 264..268
FT /evidence="ECO:0007829|PDB:2GDQ"
FT HELIX 269..283
FT /evidence="ECO:0007829|PDB:2GDQ"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:2GDQ"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:2GDQ"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:2GDQ"
FT HELIX 330..334
FT /evidence="ECO:0007829|PDB:2GDQ"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:2GDQ"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:2GDQ"
FT HELIX 358..363
FT /evidence="ECO:0007829|PDB:2GDQ"
SQ SEQUENCE 371 AA; 42052 MW; C41FD69E471FE87E CRC64;
MKIVRIETFP LFHRLEKPYG DANGFKRYRT CYLIRIITES GIDGWGECVD WLPALHVGFT
KRIIPFLLGK QAGSRLSLVR TIQKWHQRAA SAVSMALTEI AAKAADCSVC ELWGGRYREE
IPVYASFQSY SDSPQWISRS VSNVEAQLKK GFEQIKVKIG GTSFKEDVRH INALQHTAGS
SITMILDANQ SYDAAAAFKW ERYFSEWTNI GWLEEPLPFD QPQDYAMLRS RLSVPVAGGE
NMKGPAQYVP LLSQRCLDII QPDVMHVNGI DEFRDCLQLA RYFGVRASAH AYDGSLSRLY
ALFAQACLPP WSKMKNDHIE PIEWDVMENP FTDLVSLQPS KGMVHIPKGK GIGTEINMEI
VNRYKWDGSA Y
