HUTI_AERHH
ID HUTI_AERHH Reviewed; 411 AA.
AC A0KF84;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 99.
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=AHA_0377;
OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=380703;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC
RC 2358 / NCIMB 9240 / NCTC 8049;
RX PubMed=16980456; DOI=10.1128/jb.00621-06;
RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL J. Bacteriol. 188:8272-8282(2006).
RN [2] {ECO:0007744|PDB:2OOF}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 6-411 IN COMPLEX WITH IRON IONS.
RA Tyagi R., Eswaramoorthy S., Burley S.K., Swaminathan S.;
RT "The crystal structure of 4-imidazolone-5-propanoate amidohydrolase from
RT environmental sample.";
RL Submitted (JAN-2007) to the PDB data bank.
RN [3] {ECO:0007744|PDB:2Q09}
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 6-411 IN COMPLEX WITH IRON IONS
RP AND SUBSTRATE ANALOG 3-(2,5-DIOXO-IMIDAZOLIDIN-4-YL)-PROPANOATE.
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:18442260, ECO:0000305|Ref.2};
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 -!- SEQUENCE CAUTION:
CC Sequence=ABK39901.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000462; ABK39901.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_854906.1; NC_008570.1.
DR PDB; 2OOF; X-ray; 2.20 A; A=6-411.
DR PDB; 2Q09; X-ray; 1.97 A; A=6-411.
DR PDBsum; 2OOF; -.
DR PDBsum; 2Q09; -.
DR AlphaFoldDB; A0KF84; -.
DR SMR; A0KF84; -.
DR STRING; 380703.AHA_0377; -.
DR EnsemblBacteria; ABK39901; ABK39901; AHA_0377.
DR KEGG; aha:AHA_0377; -.
DR PATRIC; fig|380703.7.peg.364; -.
DR eggNOG; COG1228; Bacteria.
DR HOGENOM; CLU_041647_0_0_6; -.
DR UniPathway; UPA00379; UER00551.
DR EvolutionaryTrace; A0KF84; -.
DR Proteomes; UP000000756; 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; 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..411
FT /note="Imidazolonepropionase"
FT /id="PRO_0000306422"
FT BINDING 75
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:18442260,
FT ECO:0007744|PDB:2OOF, ECO:0007744|PDB:2Q09"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 77
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:18442260,
FT ECO:0007744|PDB:2OOF, ECO:0007744|PDB:2Q09"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 84
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000305|PubMed:18442260,
FT ECO:0007744|PDB:2Q09"
FT BINDING 147
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000305|PubMed:18442260,
FT ECO:0007744|PDB:2Q09"
FT BINDING 147
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 180
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000305|PubMed:18442260,
FT ECO:0007744|PDB:2Q09"
FT BINDING 245
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:18442260,
FT ECO:0007744|PDB:2OOF, ECO:0007744|PDB:2Q09"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 248
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000305|PubMed:18442260,
FT ECO:0007744|PDB:2Q09"
FT BINDING 320
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:18442260,
FT ECO:0007744|PDB:2OOF, ECO:0007744|PDB:2Q09"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 322
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
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 325
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000305|PubMed:18442260,
FT ECO:0007744|PDB:2Q09"
FT STRAND 9..18
FT /evidence="ECO:0007829|PDB:2Q09"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:2Q09"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:2Q09"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2Q09"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2Q09"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:2Q09"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:2Q09"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:2Q09"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:2Q09"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:2Q09"
FT HELIX 119..135
FT /evidence="ECO:0007829|PDB:2Q09"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:2Q09"
FT HELIX 151..167
FT /evidence="ECO:0007829|PDB:2Q09"
FT STRAND 168..179
FT /evidence="ECO:0007829|PDB:2Q09"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:2Q09"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:2Q09"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:2Q09"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:2Q09"
FT HELIX 225..237
FT /evidence="ECO:0007829|PDB:2Q09"
FT STRAND 241..249
FT /evidence="ECO:0007829|PDB:2Q09"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:2Q09"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:2Q09"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:2Q09"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:2Q09"
FT HELIX 291..296
FT /evidence="ECO:0007829|PDB:2Q09"
FT HELIX 305..310
FT /evidence="ECO:0007829|PDB:2Q09"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:2Q09"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:2Q09"
FT HELIX 331..342
FT /evidence="ECO:0007829|PDB:2Q09"
FT HELIX 346..352
FT /evidence="ECO:0007829|PDB:2Q09"
FT HELIX 355..360
FT /evidence="ECO:0007829|PDB:2Q09"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:2Q09"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:2Q09"
FT STRAND 378..384
FT /evidence="ECO:0007829|PDB:2Q09"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:2Q09"
FT STRAND 398..403
FT /evidence="ECO:0007829|PDB:2Q09"
SQ SEQUENCE 411 AA; 44543 MW; 63D38DB562DC8EBF CRC64;
MNKELLNCER VWLNVTPATL RSDLADYGLL EPHALGVHEG RIHALVPMQD LKGPYPAHWQ
DMKGKLVTPG LIDCHTHLIF AGSRAEEFEL RQKGVPYAEI ARKGGGIIST VRATRAACEE
QLFELALPRV KSLIREGVTT VEIKSGYGLT LEDELKMLRV ARRLGEALPI RVKTTLLAAH
AVPPEYRDDP DSWVETICQE IIPAAAEAGL ADAVDVFCEH IGFSLAQTEQ VYLAADQYGL
AVKGHMDQLS NLGGSTLAAN FGALSVDHLE YLDPEGIQAL AHRGVVATLL PTAFYFLKET
KLPPVAALRK AGVPMAVSSD INPGTAPIVS LRMAMNMACT LFGLTPVEAM AGVTRHAARA
LGEQEQLGQL RVGMLADFLV WNCGHPAELS YLIGVDQLVS RVINGEETLH G
