HUTI_SYNFM
ID HUTI_SYNFM Reviewed; 424 AA.
AC A0LKV6;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Sfum_2377;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000478; ABK18058.1; -; Genomic_DNA.
DR RefSeq; WP_011699226.1; NC_008554.1.
DR AlphaFoldDB; A0LKV6; -.
DR SMR; A0LKV6; -.
DR STRING; 335543.Sfum_2377; -.
DR EnsemblBacteria; ABK18058; ABK18058; Sfum_2377.
DR KEGG; sfu:Sfum_2377; -.
DR eggNOG; COG1228; Bacteria.
DR HOGENOM; CLU_041647_0_1_7; -.
DR OMA; CAPHARW; -.
DR OrthoDB; 785930at2; -.
DR UniPathway; UPA00379; UER00551.
DR Proteomes; UP000001784; Chromosome.
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 3: Inferred from homology;
KW Cytoplasm; Histidine metabolism; Hydrolase; Iron; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..424
FT /note="Imidazolonepropionase"
FT /id="PRO_0000306532"
FT BINDING 81
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 83
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 90
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 153
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 153
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 186
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 251
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 254
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 424 AA; 45592 MW; 566E7FA9553B32BF CRC64;
MSRKLFRNGR IFTPTDRGVP LAGKHQGDVI HIPRGAIYAK DGVIEAVGDE REVLAGISAG
QVDEEIDCRG YCVIPGFVDP HTHMCFAKTR EEEFLLRIEG MEYLEILGRG GGILSSVRAA
RAATEDELFA FTRKHVMTAL GLGTTTLEIK SGYGLDTESE LRMLRVIERI GRETPLDVVP
TFLGAHAIPE EHVAHPDGYV DLVVHEMLPA VARHSGAVFC DVFCEAGVFS VAQSRRVLEA
ARGVGLELKI HTDEVHDLGG SALAAELRAT SAEHLLRTSE TNLRAMAEAG VVGILLPATA
YSLRRRYAPA RRMVELGLPV AVATDCNPGT AYTESMPFVY GLAVLGMGLS MQEALVAATL
NGAYAIGQGG RVGSLEVGKS ADFLLLDGKS PAILAYHIGV SPVVEVYKQA NPMRQWEGIT
GDHP
