HUTI_BACSU
ID HUTI_BACSU Reviewed; 421 AA.
AC P42084;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Imidazolonepropionase {ECO:0000255|HAMAP-Rule:MF_00372, ECO:0000303|PubMed:16990261};
DE EC=3.5.2.7 {ECO:0000255|HAMAP-Rule:MF_00372, ECO:0000305|PubMed:27711543};
DE AltName: Full=Imidazolone-5-propionate hydrolase {ECO:0000255|HAMAP-Rule:MF_00372};
GN Name=hutI {ECO:0000255|HAMAP-Rule:MF_00372}; OrderedLocusNames=BSU39370;
GN ORFNames=EE57B;
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 / BGSC1A1;
RX PubMed=7704263; DOI=10.1099/13500872-141-2-337;
RA Yoshida K., Sano H., Seki S., Oda M., Fujimura M., Fujita Y.;
RT "Cloning and sequencing of a 29 kb region of the Bacillus subtilis genome
RT containing the hut and wapA loci.";
RL Microbiology 141:337-343(1995).
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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27711543; DOI=10.1039/c6cp04918d;
RA Su H., Sheng X., Liu Y.;
RT "Exploring the substrate specificity and catalytic mechanism of
RT imidazolonepropionase (HutI) from Bacillus subtilis.";
RL Phys. Chem. Chem. Phys. 18:27928-27938(2016).
RN [4] {ECO:0007744|PDB:2BB0, ECO:0007744|PDB:2G3F}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOG
RP IMIDAZOLE-4-ACETATE AND ZINC IONS, AND SUBUNIT.
RX PubMed=16990261; DOI=10.1074/jbc.m607703200;
RA Yu Y., Liang Y.-H., Brostromer E., Quan J.-M., Panjikar S., Dong Y.-H.,
RA Su X.-D.;
RT "A catalytic mechanism revealed by the crystal structures of the
RT imidazolonepropionase from Bacillus subtilis.";
RL J. Biol. Chem. 281:36929-36936(2006).
CC -!- FUNCTION: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond
CC in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is
CC the third step in the universal histidine degradation pathway.
CC {ECO:0000255|HAMAP-Rule:MF_00372, ECO:0000305|PubMed:27711543}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-imidazolone-5-propanoate + H2O = N-formimidoyl-L-glutamate;
CC Xref=Rhea:RHEA:23660, ChEBI:CHEBI:15377, ChEBI:CHEBI:58928,
CC ChEBI:CHEBI:77893; EC=3.5.2.7; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00372, ECO:0000305|PubMed:27711543};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00372,
CC ECO:0000305|PubMed:27711543};
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00372};
CC Note=Binds 1 zinc or iron ion per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00372};
CC -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
CC {ECO:0000255|HAMAP-Rule:MF_00372}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16990261}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00372}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC HutI family. {ECO:0000255|HAMAP-Rule:MF_00372}.
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DR EMBL; D31856; BAA06642.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15973.1; -; Genomic_DNA.
DR PIR; D69643; D69643.
DR RefSeq; NP_391816.1; NC_000964.3.
DR RefSeq; WP_003244327.1; NZ_JNCM01000034.1.
DR PDB; 2BB0; X-ray; 2.00 A; A/B=1-421.
DR PDB; 2G3F; X-ray; 2.00 A; A/B=1-421.
DR PDBsum; 2BB0; -.
DR PDBsum; 2G3F; -.
DR AlphaFoldDB; P42084; -.
DR SMR; P42084; -.
DR STRING; 224308.BSU39370; -.
DR PaxDb; P42084; -.
DR PRIDE; P42084; -.
DR EnsemblBacteria; CAB15973; CAB15973; BSU_39370.
DR GeneID; 937531; -.
DR KEGG; bsu:BSU39370; -.
DR PATRIC; fig|224308.179.peg.4262; -.
DR eggNOG; COG1228; Bacteria.
DR InParanoid; P42084; -.
DR OMA; CAPHARW; -.
DR PhylomeDB; P42084; -.
DR BioCyc; BSUB:BSU39370-MON; -.
DR BioCyc; MetaCyc:HUTIBACSU-MON; -.
DR BRENDA; 3.5.2.7; 658.
DR UniPathway; UPA00379; UER00551.
DR EvolutionaryTrace; P42084; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050480; F:imidazolonepropionase activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006548; P:histidine catabolic process; IBA:GO_Central.
DR GO; GO:0019556; P:histidine catabolic process to glutamate and formamide; IEA:UniProtKB-UniPathway.
DR GO; GO:0019557; P:histidine catabolic process to glutamate and formate; IEA:UniProtKB-UniPathway.
DR CDD; cd01296; Imidazolone-5PH; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR HAMAP; MF_00372; HutI; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR005920; HutI.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR42752; PTHR42752; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 2.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01224; hutI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Histidine metabolism; Hydrolase; Iron;
KW Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..421
FT /note="Imidazolonepropionase"
FT /id="PRO_0000160944"
FT BINDING 80
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16990261,
FT ECO:0007744|PDB:2BB0, ECO:0007744|PDB:2G3F"
FT BINDING 82
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16990261,
FT ECO:0007744|PDB:2BB0, ECO:0007744|PDB:2G3F"
FT BINDING 89
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000305|PubMed:16990261,
FT ECO:0007744|PDB:2G3F"
FT BINDING 152
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000305|PubMed:16990261,
FT ECO:0007744|PDB:2G3F"
FT BINDING 152
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 185
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000305|PubMed:16990261,
FT ECO:0007744|PDB:2G3F"
FT BINDING 249
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16990261,
FT ECO:0007744|PDB:2BB0, ECO:0007744|PDB:2G3F"
FT BINDING 252
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000305|PubMed:16990261,
FT ECO:0007744|PDB:2G3F"
FT BINDING 324
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16990261,
FT ECO:0007744|PDB:2BB0, ECO:0007744|PDB:2G3F"
FT BINDING 326
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 328
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 329
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT STRAND 4..15
FT /evidence="ECO:0007829|PDB:2BB0"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:2BB0"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:2BB0"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:2BB0"
FT TURN 53..58
FT /evidence="ECO:0007829|PDB:2BB0"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:2BB0"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:2BB0"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2BB0"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:2BB0"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:2BB0"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:2BB0"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:2BB0"
FT HELIX 124..140
FT /evidence="ECO:0007829|PDB:2BB0"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:2BB0"
FT HELIX 156..172
FT /evidence="ECO:0007829|PDB:2BB0"
FT STRAND 173..186
FT /evidence="ECO:0007829|PDB:2BB0"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:2BB0"
FT HELIX 195..203
FT /evidence="ECO:0007829|PDB:2BB0"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:2BB0"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:2BB0"
FT HELIX 229..241
FT /evidence="ECO:0007829|PDB:2BB0"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:2BB0"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2BB0"
FT HELIX 258..264
FT /evidence="ECO:0007829|PDB:2BB0"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:2BB0"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:2BB0"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:2BB0"
FT HELIX 295..300
FT /evidence="ECO:0007829|PDB:2BB0"
FT HELIX 309..314
FT /evidence="ECO:0007829|PDB:2BB0"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:2BB0"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:2BB0"
FT HELIX 335..345
FT /evidence="ECO:0007829|PDB:2BB0"
FT HELIX 350..356
FT /evidence="ECO:0007829|PDB:2BB0"
FT HELIX 359..364
FT /evidence="ECO:0007829|PDB:2BB0"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:2BB0"
FT STRAND 382..389
FT /evidence="ECO:0007829|PDB:2BB0"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:2BB0"
FT STRAND 402..407
FT /evidence="ECO:0007829|PDB:2BB0"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:2BB0"
SQ SEQUENCE 421 AA; 45564 MW; A0E1893961745771 CRC64;
MPKQIDTILI NIGQLLTMES SGPRAGKSMQ DLHVIEDAVV GIHEQKIVFA GQKGAEAGYE
ADEIIDCSGR LVTPGLVDPH THLVFGGSRE KEMNLKLQGI SYLDILAQGG GILSTVKDTR
AASEEELLQK AHFHLQRMLS YGTTTAEVKS GYGLEKETEL KQLRVAKKLH ESQPVDLVST
FMGAHAIPPE YQNDPDDFLD QMLSLLPEIK EQELASFADI FTETGVFTVS QSRRYLQKAA
EAGFGLKIHA DEIDPLGGAE LAGKLKAVSA DHLVGTSDEG IKKLAEAGTI AVLLPGTTFY
LGKSTYARAR AMIDEGVCVS LATDFNPGSS PTENIQLIMS IAALHLKMTA EEIWHAVTVN
AAYAIGKGEE AGQLKAGRSA DLVIWQAPNY MYIPYHYGVN HVHQVMKNGT IVVNREGAIL
G
