HUTI_AGRFC
ID HUTI_AGRFC Reviewed; 419 AA.
AC Q8U8Z6;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Imidazolonepropionase {ECO:0000255|HAMAP-Rule:MF_00372, ECO:0000303|PubMed:17640072, ECO:0000303|PubMed:18442260};
DE EC=3.5.2.7 {ECO:0000255|HAMAP-Rule:MF_00372};
DE AltName: Full=Imidazolone-5-propanoate hydrolase {ECO:0000303|PubMed:18442260};
DE AltName: Full=Imidazolone-5-propionate hydrolase {ECO:0000255|HAMAP-Rule:MF_00372};
GN Name=hutI {ECO:0000255|HAMAP-Rule:MF_00372, ECO:0000303|PubMed:18442260};
GN OrderedLocusNames=Atu3934; ORFNames=AGR_L_1824;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
RN [3] {ECO:0007744|PDB:2GOK}
RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) IN COMPLEX WITH IRON IONS, AND
RP SUBUNIT.
RX PubMed=17640072; DOI=10.1002/prot.21559;
RA Tyagi R., Kumaran D., Burley S.K., Swaminathan S.;
RT "X-ray structure of imidazolonepropionase from Agrobacterium tumefaciens at
RT 1.87 A resolution.";
RL Proteins 69:652-658(2007).
RN [4] {ECO:0007744|PDB:2PUZ}
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) IN COMPLEX WITH
RP N-FORMIMIDOYL-L-GLUTAMATE AND IRON IONS.
RX PubMed=18442260; DOI=10.1021/bi800180g;
RA Tyagi R., Eswaramoorthy S., Burley S.K., Raushel F.M., Swaminathan S.;
RT "A common catalytic mechanism for proteins of the HutI family.";
RL Biochemistry 47:5608-5615(2008).
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:0000305|PubMed:17640072, ECO:0000305|PubMed:18442260};
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: Monomer. Forms a tightly packed homodimer in the crystal, but
CC this seems to be an artifact of crystallization.
CC {ECO:0000269|PubMed:17640072}.
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; AE007870; AAK89486.2; -; Genomic_DNA.
DR PIR; AH3040; AH3040.
DR PIR; D98245; D98245.
DR RefSeq; NP_356701.2; NC_003063.2.
DR RefSeq; WP_010973444.1; NC_003063.2.
DR PDB; 2GOK; X-ray; 1.87 A; A/B=2-419.
DR PDB; 2PUZ; X-ray; 1.83 A; A/B=1-419.
DR PDBsum; 2GOK; -.
DR PDBsum; 2PUZ; -.
DR AlphaFoldDB; Q8U8Z6; -.
DR SMR; Q8U8Z6; -.
DR STRING; 176299.Atu3934; -.
DR MEROPS; M38.980; -.
DR EnsemblBacteria; AAK89486; AAK89486; Atu3934.
DR GeneID; 66224190; -.
DR KEGG; atu:Atu3934; -.
DR PATRIC; fig|176299.10.peg.3757; -.
DR eggNOG; COG1228; Bacteria.
DR HOGENOM; CLU_041647_0_0_5; -.
DR OMA; CAPHARW; -.
DR PhylomeDB; Q8U8Z6; -.
DR BioCyc; AGRO:ATU3934-MON; -.
DR BRENDA; 3.5.2.7; 200.
DR UniPathway; UPA00379; UER00551.
DR EvolutionaryTrace; Q8U8Z6; -.
DR Proteomes; UP000000813; Chromosome linear.
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 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; 1.
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..419
FT /note="Imidazolonepropionase"
FT /id="PRO_0000160942"
FT BINDING 84
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:17640072,
FT ECO:0000269|PubMed:18442260, ECO:0007744|PDB:2GOK,
FT ECO:0007744|PDB:2PUZ"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 86
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:17640072,
FT ECO:0000269|PubMed:18442260, ECO:0007744|PDB:2GOK,
FT ECO:0007744|PDB:2PUZ"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 93
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 156
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 156
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000269|PubMed:18442260,
FT ECO:0007744|PDB:2PUZ"
FT BINDING 189
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 254
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:17640072,
FT ECO:0000269|PubMed:18442260, ECO:0007744|PDB:2GOK,
FT ECO:0007744|PDB:2PUZ"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 257
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 329
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:17640072,
FT ECO:0000269|PubMed:18442260, ECO:0007744|PDB:2GOK,
FT ECO:0007744|PDB:2PUZ"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 331
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000269|PubMed:18442260,
FT ECO:0007744|PDB:2PUZ"
FT BINDING 333
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000269|PubMed:18442260,
FT ECO:0007744|PDB:2PUZ"
FT BINDING 334
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT STRAND 16..25
FT /evidence="ECO:0007829|PDB:2PUZ"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:2PUZ"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:2PUZ"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:2PUZ"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:2PUZ"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:2PUZ"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2PUZ"
FT HELIX 94..101
FT /evidence="ECO:0007829|PDB:2PUZ"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:2PUZ"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:2PUZ"
FT HELIX 128..143
FT /evidence="ECO:0007829|PDB:2PUZ"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:2PUZ"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:2PUZ"
FT HELIX 160..173
FT /evidence="ECO:0007829|PDB:2PUZ"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:2PUZ"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:2PUZ"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:2PUZ"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:2PUZ"
FT HELIX 207..216
FT /evidence="ECO:0007829|PDB:2PUZ"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:2PUZ"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:2PUZ"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:2PUZ"
FT STRAND 251..259
FT /evidence="ECO:0007829|PDB:2PUZ"
FT HELIX 263..269
FT /evidence="ECO:0007829|PDB:2PUZ"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:2PUZ"
FT HELIX 283..292
FT /evidence="ECO:0007829|PDB:2PUZ"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:2PUZ"
FT HELIX 300..306
FT /evidence="ECO:0007829|PDB:2PUZ"
FT HELIX 314..320
FT /evidence="ECO:0007829|PDB:2PUZ"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:2PUZ"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:2PUZ"
FT HELIX 340..351
FT /evidence="ECO:0007829|PDB:2PUZ"
FT HELIX 355..361
FT /evidence="ECO:0007829|PDB:2PUZ"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:2PUZ"
FT TURN 373..375
FT /evidence="ECO:0007829|PDB:2PUZ"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:2PUZ"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:2PUZ"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:2PUZ"
FT STRAND 407..412
FT /evidence="ECO:0007829|PDB:2PUZ"
SQ SEQUENCE 419 AA; 44400 MW; 55D09461815693CF CRC64;
MPGNNSAKGT ATGNATALWR NAQLATLNPA MDGIGAVENA VIAVRNGRIA FAGPESDLPD
DLSTADETTD CGGRWITPAL IDCHTHLVFG GNRAMEFEMR LNGATYEEIA KAGGGIVSSV
RDTRALSDEV LVAQALPRLD TLLSEGVSTI EIKSGYGLDI ETELKMLRVA RRLETLRPVR
IVTSYLAAHA TPADYKGRNA DYITDVVLPG LEKAHAEGLA DAVDGFCEGI AFSVKEIDRV
FAAAQQRGLP VKLHAEQLSN LGGAELAASY NALSADHLEY LDETGAKALA KAGTVAVLLP
GAFYALREKQ LPPVQALRDA GAEIALATDC NPGTSPLTSL LLTMNMGATL FRMTVEECLT
ATTRNAAKAL GLLAETGTLE AGKSADFAIW DIERPAELVY RIGFNPLHAR IFKGQKVSP
