HUTI_FLAJ1
ID HUTI_FLAJ1 Reviewed; 411 AA.
AC A5FB49;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Fjoh_4570;
OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=376686;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101;
RX PubMed=19717629; DOI=10.1128/aem.01495-09;
RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA Cheng Y.Q., Stein J.L.;
RT "Novel features of the polysaccharide-digesting gliding bacterium
RT Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL Appl. Environ. Microbiol. 75:6864-6875(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}.
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DR EMBL; CP000685; ABQ07569.1; -; Genomic_DNA.
DR RefSeq; WP_012026535.1; NZ_MUGZ01000011.1.
DR AlphaFoldDB; A5FB49; -.
DR SMR; A5FB49; -.
DR STRING; 376686.Fjoh_4570; -.
DR EnsemblBacteria; ABQ07569; ABQ07569; Fjoh_4570.
DR KEGG; fjo:Fjoh_4570; -.
DR eggNOG; COG1228; Bacteria.
DR HOGENOM; CLU_041647_0_1_10; -.
DR OMA; CAPHARW; -.
DR OrthoDB; 785930at2; -.
DR UniPathway; UPA00379; UER00551.
DR Proteomes; UP000006694; 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; Zinc.
FT CHAIN 1..411
FT /note="Imidazolonepropionase"
FT /id="PRO_1000079822"
FT BINDING 78
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
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 87
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 150
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 150
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 183
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 248
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 251
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 322
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 324
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
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 327
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
SQ SEQUENCE 411 AA; 45076 MW; A4542F936046042F CRC64;
MITLIKNIQE LLQVRQTSIS KVSGAEMAEL PTIKNAFLVI KDDLIADFGS MENLPEIKAD
SIINASGRVV LPAWCDSHTH IVYAGNREQE FVDRINGFTY EEIANRGGGI LNSAKKLNET
SEEEIYEQSK IRLEEVMRLG TGAVEIKSGY GLTVEGELKM LRVIKKLAEN YPISIKATFL
GAHAFPTHYK ENKAGYIDEI ITKMLPEIAQ NKLADYVDVF CESGYFSVEE TEKIMQAGID
FGLKPKIHVN QFNSIGGIQS GVKFNALSVD HLEIMNPEDI EALKGTETMP VALPSCSYFL
SIPYTPAREM IKAGLPLALA TDFNPGSTPS GNMNFVVATA CIKMKMTPEE AINAATINGA
YAMGLSETHG SITKGKKANL IITKPISSYY QIPYAFGSNL IEDVLIDGQI I
