HUTI_XANOR
ID HUTI_XANOR Reviewed; 879 AA.
AC Q5H071;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Imidazolonepropionase;
DE EC=3.5.2.7;
DE AltName: Full=Imidazolone-5-propionate hydrolase;
GN Name=hutI; OrderedLocusNames=XOO2396;
OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=291331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC10331 / KXO85;
RX PubMed=15673718; DOI=10.1093/nar/gki206;
RA Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA Go S.-J.;
RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT bacterial blight pathogen of rice.";
RL Nucleic Acids Res. 33:577-586(2005).
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;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250};
CC Note=Binds 1 zinc or iron ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC HutI family. {ECO:0000305}.
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DR EMBL; AE013598; AAW75650.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5H071; -.
DR SMR; Q5H071; -.
DR STRING; 291331.XOO2396; -.
DR PRIDE; Q5H071; -.
DR EnsemblBacteria; AAW75650; AAW75650; XOO2396.
DR KEGG; xoo:XOO2396; -.
DR HOGENOM; CLU_327306_0_0_6; -.
DR UniPathway; UPA00379; UER00551.
DR Proteomes; UP000006735; 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 Gene3D; 2.30.40.10; -; 1.
DR HAMAP; MF_00372; HutI; 1.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR005920; HutI.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR42752; PTHR42752; 1.
DR Pfam; PF07969; Amidohydro_3; 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..879
FT /note="Imidazolonepropionase"
FT /id="PRO_0000306538"
FT REGION 1..478
FT /note="Unknown"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..879
FT /note="Imidazolonepropionase"
FT BINDING 548
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 548
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 550
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 550
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 557
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 620
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 620
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 653
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 716
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 716
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 719
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 791
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 791
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 793
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 795
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 796
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
SQ SEQUENCE 879 AA; 94673 MW; DD7D21CB5CC3105A CRC64;
MSCVQQAAQH RSKPRGNTRA IGMPPIAHHP APAAPDIAYR RATRGEQPAV YQGVVVARQQ
GRMRCVQLDQ ISRGTGTDAG VRNAQRLRGT NAGLIVEPAS AGYSTLRHYI ARLQRQALAV
FEQAQFFGCI DQHIRIRAHA EASARRGKCP HREHAVAQIR LGDRAQTDDR AAGDDRLQFV
RIHVRGVHQT PARIHRRVGQ QPLHRTLPGP GQAGIHFTLL FGDMDVDGAI GERHQRRQLR
RGDRTQAVRR QPKHRIRQRF QAVSAVVQQA CETIDAVNQA ALRRAGSGTA EIRMRIEHRQ
QAETDAGVGG RGGDALGHFA GMRVRRTAHG VVQIVEFADA GEAAFEHFHI RLFGDRLQAV
RIEPVDEAVH QLAPAPEAVA AASADFGQPR HAALEGMAVQ IAQARQQHVA ARVGQGSSGT
GLQRGDAALL CRDPHPARPA VGQQRPGGPE HLHLLVSHWT PSIAELIVYT YQTPRACAMH
CDVLWHNAQL MTLDAADGGL GIVDDGTVAC QQGRIVYAGP AAQAPALQPH ATHDCQRRWI
SPGLIDCHTH LVYAGNRANE FEQRLRGASY ADIAAAGGGI VATVRATRAA DDAALLAASL
PRLDAMLGEG VTTLEIKSGY GLTLDDEIKQ LRVARQLAAL RKVEVVPTFL GAHAVPPGGD
AQRYTDQVCT QMIPAIAAQG LAEAVDVFCE HLAFSHAQAE QVFIAAQAHG LHIKIHAEQL
SNQHGAELAA RYGALSADHI EYLDQAGIAA MAGAGTVAVL LPGAFYFTRD TQVPPIAALR
AAGVPLALAT DCNPGTSPLT SPLLAMNMAA TLFRMTVDEC IAGFTREAAR ALGRSERLGR
LRAGMDCDLA IWDIDAPADL VYRMGFNPLH ARVLRGHLC
