(data stored in ACNUC7421 zone)

SWISSPROT: C7QJ61_CATAD

ID   C7QJ61_CATAD            Unreviewed;       393 AA.
AC   C7QJ61;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   30-AUG-2017, entry version 64.
DE   RecName: Full=Imidazolonepropionase {ECO:0000256|HAMAP-Rule:MF_00372, ECO:0000256|SAAS:SAAS00381179};
DE            EC=3.5.2.7 {ECO:0000256|HAMAP-Rule:MF_00372, ECO:0000256|SAAS:SAAS00381179};
DE   AltName: Full=Imidazolone-5-propionate hydrolase {ECO:0000256|HAMAP-Rule:MF_00372};
GN   Name=hutI {ECO:0000256|HAMAP-Rule:MF_00372};
GN   OrderedLocusNames=Caci_0250 {ECO:0000313|EMBL:ACU69203.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69203.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69203.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
CC   -!- CATALYTIC ACTIVITY: (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-
CC       yl)propanoate + H(2)O = N-formimidoyl-L-glutamate + H(+).
CC       {ECO:0000256|HAMAP-Rule:MF_00372, ECO:0000256|SAAS:SAAS00381182}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|SAAS:SAAS00611463};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00372};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00372};
CC       Note=Binds 1 zinc or iron ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00372, ECO:0000256|SAAS:SAAS00381190}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00372}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. HutI family. {ECO:0000256|HAMAP-Rule:MF_00372,
CC       ECO:0000256|SAAS:SAAS00852831}.
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DR   EMBL; CP001700; ACU69203.1; -; Genomic_DNA.
DR   ProteinModelPortal; C7QJ61; -.
DR   STRING; 479433.Caci_0250; -.
DR   EnsemblBacteria; ACU69203; ACU69203; Caci_0250.
DR   KEGG; cai:Caci_0250; -.
DR   eggNOG; ENOG4105CI2; Bacteria.
DR   eggNOG; COG1228; LUCA.
DR   HOGENOM; HOG000218460; -.
DR   KO; K01468; -.
DR   OMA; CMMRAGT; -.
DR   OrthoDB; POG091H0EIK; -.
DR   UniPathway; UPA00379; UER00551.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050480; F:imidazolonepropionase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
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; -; 2.
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; 2.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01224; hutI; 1.
PE   3: Inferred from homology;
DR   PRODOM; C7QJ61.
DR   SWISS-2DPAGE; C7QJ61.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00372};
KW   Histidine metabolism {ECO:0000256|HAMAP-Rule:MF_00372,
KW   ECO:0000256|SAAS:SAAS00458442};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00372,
KW   ECO:0000256|SAAS:SAAS00458430, ECO:0000313|EMBL:ACU69203.1};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00372, ECO:0000256|SAAS:SAAS00458452};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00372,
KW   ECO:0000256|SAAS:SAAS00458441};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00372, ECO:0000256|SAAS:SAAS00458440}.
FT   DOMAIN       65    389       Amidohydro-rel. {ECO:0000259|Pfam:
FT                                PF01979}.
FT   METAL        73     73       Zinc or iron. {ECO:0000256|HAMAP-Rule:
FT                                MF_00372}.
FT   METAL        75     75       Zinc or iron. {ECO:0000256|HAMAP-Rule:
FT                                MF_00372}.
FT   METAL       230    230       Zinc or iron. {ECO:0000256|HAMAP-Rule:
FT                                MF_00372}.
FT   METAL       304    304       Zinc or iron. {ECO:0000256|HAMAP-Rule:
FT                                MF_00372}.
FT   BINDING      82     82       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00372}.
FT   BINDING      95     95       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00372}.
FT   BINDING     140    140       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00372}.
FT   BINDING     167    167       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00372}.
FT   BINDING     233    233       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00372}.
SQ   SEQUENCE   393 AA;  41140 MW;  5688E06A8A294D7A CRC64;
     MGSSVTSTLL TGIAELTTHA DSGGLADSTV ADAAMVVVDG RVAWTGPGAG APDADERVEL
     GGRAVIPGFV DSHAHLVFAG DRAQEFAARM TGAPYSAGGI RTTVAATRGA SDDVLRSNLR
     RLVGEMLRQG TTTVECKSGY GLTVEDEARA LRLAREQVEA VTYLGAHVVP AEYKDRAGEY
     VDLVKGPMLD ACAPYADFAD VFCERGAFDE EQTREILTAA RAKGLDLRLH ANQLGNGPGV
     QLAVEFGAAS ADHCTFLDDK DIDALAGSQT IATLLPGVEF STRSPYPDAR RLLDAGATVA
     IATDCNPGSC YTNSMPFCIA VAVRDMHMSP AEALWAATVG GAKALRRDDV GHLGVGARAD
     FAVLDAPSYL HLAYRPGVPL VHRVWKNGTP VAG
//

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