HUTIH_BRUME
ID HUTIH_BRUME Reviewed; 925 AA.
AC Q8YD09;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Bifunctional imidazolonepropionase/histidine ammonia-lyase;
DE Includes:
DE RecName: Full=Imidazolonepropionase;
DE EC=3.5.2.7;
DE AltName: Full=Imidazolone-5-propionate hydrolase;
DE Includes:
DE RecName: Full=Histidine ammonia-lyase;
DE Short=Histidase;
DE EC=4.3.1.3;
GN Name=hutIH; OrderedLocusNames=BMEII0368;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidine = NH4(+) + trans-urocanate; Xref=Rhea:RHEA:21232,
CC ChEBI:CHEBI:17771, ChEBI:CHEBI:28938, ChEBI:CHEBI:57595; EC=4.3.1.3;
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 1/3.
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:0000305}.
CC -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which
CC is formed autocatalytically by cyclization and dehydration of residues
CC Ala-Ser-Gly. {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the metallo-dependent
CC hydrolases superfamily. HutI family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PAL/histidase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL53610.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE008918; AAL53610.1; ALT_FRAME; Genomic_DNA.
DR PIR; AG3555; AG3555.
DR STRING; 224914.BMEII0368; -.
DR EnsemblBacteria; AAL53610; AAL53610; BMEII0368.
DR KEGG; bme:BMEII0368; -.
DR eggNOG; COG1228; Bacteria.
DR eggNOG; COG2986; Bacteria.
DR UniPathway; UPA00379; UER00549.
DR UniPathway; UPA00379; UER00551.
DR Proteomes; UP000000419; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004397; F:histidine ammonia-lyase activity; IEA:UniProtKB-UniRule.
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 CDD; cd00332; PAL-HAL; 1.
DR Gene3D; 1.10.275.10; -; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR HAMAP; MF_00229; His_ammonia_lyase; 1.
DR HAMAP; MF_00372; HutI; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR001106; Aromatic_Lyase.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR005921; HutH.
DR InterPro; IPR005920; HutI.
DR InterPro; IPR008948; L-Aspartase-like.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR022313; Phe/His_NH3-lyase_AS.
DR PANTHER; PTHR10362; PTHR10362; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF00221; Lyase_aromatic; 1.
DR SUPFAM; SSF48557; SSF48557; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01225; hutH; 1.
DR TIGRFAMs; TIGR01224; hutI; 1.
DR PROSITE; PS00488; PAL_HISTIDASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Histidine metabolism; Hydrolase; Iron; Lyase; Metal-binding;
KW Multifunctional enzyme; Zinc.
FT CHAIN 1..925
FT /note="Bifunctional imidazolonepropionase/histidine
FT ammonia-lyase"
FT /id="PRO_0000160981"
FT REGION 1..414
FT /note="Imidazolonepropionase"
FT REGION 415..925
FT /note="Histidine ammonia-lyase"
FT BINDING 73
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 75
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 82
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 145
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 145
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 178
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 243
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 246
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 318
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 320
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
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 323
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT MOD_RES 557
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000250"
FT CROSSLNK 556..558
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 925 AA; 97849 MW; 3D7D858028548835 CRC64;
MTKNSSTVFT HARIATLEEK AANLGLIEEA ALVVKDARIV YAGPENKLPD EYASFEKIDC
GNRLITPGLI DCHTHLVHAG NRAHEFELRL QGATYEEVAR AGGGIVSSVR NLRAASEDDL
VRETLPRLDA LIAEGVTTVE VKSGYGLDRD SEIKSLKAAR RLGEERDVAI RTTFLGAHAL
PPEMNGDKAA YIDRVINDML PAIAEQGLAD AVDGFCEGIA FLPDEIARVF DAAKAHDIPV
KLHADQLSNL HGAALAASYG ALSADHLEYT DADGAAAMAS AGTVAVLLPG AYYFIRETQK
PPVEAFRAAG TKMALATDNN PGTSPLTSLL LTMNMGATLF RMTVEECIAG VTREAARALG
ILDQTGTLEI GKDADLAIWD IERPAELVYR IGFNPLWKRV FKGQIKPHVR MEPFMTIILK
PGSVPLETLE KIYREGLPVR IDPAFHAGIE KAAARIAEIA AGDAPVYGIN TGFGKLASIR
IAAGDVATLQ RNLILSHCCG VGEPLSENIV RLIMALKLVS LGRGASGVQL EVITLIEAML
EKGVIPMIPE KGSVGASGDL APLAHMTAAM IGEGEAFYRG ERLSGAKALG KAGLKPVVLA
AKEGLALING TQTSTALALA GLFRAHRAAR TALITGALST DAAMGSDAPF HEEIHQLRGH
KGQIDAGRAL RTLLEGSAIR RSHLEGDQRV QDPYCXRCQP QVDGACLDIL RQAARTLEIE
ANAVTDNPLV LSDGRAVSGG NFHAEPVAFA ADQIALAVCE IGAISQRRIA LLVDPSLSFG
LPAFLARKPG LNSGLMIAEV TSAALMSENK QMAHPASVDS TPTSANQEDH VSMACHGARR
LLQMTANLNA IIGIEALTGA LGVELRKPLT TSAELAKVIA ALRAKVATLE EDRYMADDLK
AAAELVADGT LSGVISAGIL PDLEA
