位置:首页 > 蛋白库 > HUTI_SOLUE
HUTI_SOLUE
ID   HUTI_SOLUE              Reviewed;         418 AA.
AC   Q01W05;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Imidazolonepropionase {ECO:0000255|HAMAP-Rule:MF_00372};
DE            EC=3.5.2.7 {ECO:0000255|HAMAP-Rule:MF_00372};
DE   AltName: Full=Imidazolone-5-propionate hydrolase {ECO:0000255|HAMAP-Rule:MF_00372};
GN   Name=hutI {ECO:0000255|HAMAP-Rule:MF_00372}; OrderedLocusNames=Acid_5207;
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteria; Bryobacterales; Solibacteraceae;
OC   Candidatus Solibacter.
OX   NCBI_TaxID=234267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin6076;
RX   PubMed=19201974; DOI=10.1128/aem.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
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}.
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};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00372};
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   -!- 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000473; ABJ86160.1; -; Genomic_DNA.
DR   RefSeq; WP_011686905.1; NC_008536.1.
DR   AlphaFoldDB; Q01W05; -.
DR   SMR; Q01W05; -.
DR   STRING; 234267.Acid_5207; -.
DR   EnsemblBacteria; ABJ86160; ABJ86160; Acid_5207.
DR   KEGG; sus:Acid_5207; -.
DR   eggNOG; COG1228; Bacteria.
DR   HOGENOM; CLU_041647_0_1_0; -.
DR   OMA; CAPHARW; -.
DR   OrthoDB; 785930at2; -.
DR   UniPathway; UPA00379; UER00551.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050480; F:imidazolonepropionase activity; IEA:UniProtKB-UniRule.
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: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   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; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01224; hutI; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Histidine metabolism; Hydrolase; Iron; Metal-binding; Zinc.
FT   CHAIN           1..418
FT                   /note="Imidazolonepropionase"
FT                   /id="PRO_0000306517"
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:0000255|HAMAP-Rule:MF_00372"
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:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         89
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         152
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
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:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         250
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         250
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         253
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         325
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         325
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         327
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="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         330
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
SQ   SEQUENCE   418 AA;  44759 MW;  2C77042337DAD969 CRC64;
     MSDSALLNCR QLVTLAGPPG PRTGPAMREL AIIPDGAMRI RDGCIAAVGP RADIVRSLAG
     DTEVIDAGWR VVLPGFIDAH THPVFAGTRA AEYEQRAEGA TYAEIAAAGG GIRSTVRRTR
     EAGDLELATA ARRYTDWFLR GGTTTIEAKS GYGLSLDDEL RILKTIRLLN AERRLRYVPT
     FLGAHEIPDE YRGEIEDYVD LVIQEMLPAV AEDNLAEYCD VFCEPNVFPL DPARAILQAA
     QSLGLRLRIH ADQFTGDYAA LLAAELGAAT ADHLESTTAL GLAALHEAGV QPVLLPASVY
     NLGSARYPAA RDMIARGMAV VLATDFNPGS SPTASIPMVL SLASTQMKMT PAESITAVTV
     NAAHSLGRGS RIGSLEPGKA ADFAIHECDD YRELAYFFGR EPANAVYLAG QCVYRRSA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024