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Database: UniProt
Entry: C1A4F1_GEMAT
LinkDB: C1A4F1_GEMAT
Original site: C1A4F1_GEMAT 
ID   C1A4F1_GEMAT            Unreviewed;       416 AA.
AC   C1A4F1;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 69.
DE   RecName: Full=Imidazolonepropionase {ECO:0000256|HAMAP-Rule:MF_00372};
DE            EC=3.5.2.7 {ECO:0000256|HAMAP-Rule:MF_00372};
DE   AltName: Full=Imidazolone-5-propionate hydrolase {ECO:0000256|HAMAP-Rule:MF_00372};
GN   Name=hutI {ECO:0000256|HAMAP-Rule:MF_00372,
GN   ECO:0000313|EMBL:BAH38976.1};
GN   OrderedLocusNames=GAU_1934 {ECO:0000313|EMBL:BAH38976.1};
OS   Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC
OS   100505).
OC   Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae;
OC   Gemmatimonas.
OX   NCBI_TaxID=379066 {ECO:0000313|EMBL:BAH38976.1, ECO:0000313|Proteomes:UP000002209};
RN   [1] {ECO:0000313|Proteomes:UP000002209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505
RC   {ECO:0000313|Proteomes:UP000002209};
RA   Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y.,
RA   Oguchi A., Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S.,
RA   Yokoyama H., Tanikawa S., Hanada S., Kamagata Y., Fujita N.;
RT   "Complete genome sequence of Gemmatimonas aurantiaca T-27 that
RT   represents a novel phylum Gemmatimonadetes.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-imidazolone-5-propanoate + H2O = N-formimidoyl-L-
CC         glutamate; Xref=Rhea:RHEA:23660, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:58928, ChEBI:CHEBI:77893; EC=3.5.2.7;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00372,
CC         ECO:0000256|SAAS:SAAS01124173};
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:SAAS00325479}.
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}.
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DR   EMBL; AP009153; BAH38976.1; -; Genomic_DNA.
DR   STRING; 379066.GAU_1934; -.
DR   MEROPS; M38.980; -.
DR   EnsemblBacteria; BAH38976; BAH38976; GAU_1934.
DR   KEGG; gau:GAU_1934; -.
DR   eggNOG; ENOG4105CI2; Bacteria.
DR   eggNOG; COG1228; LUCA.
DR   HOGENOM; HOG000218460; -.
DR   KO; K01468; -.
DR   OMA; PTFMGAH; -.
DR   UniPathway; UPA00379; UER00551.
DR   Proteomes; UP000002209; 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   Complete proteome {ECO:0000313|Proteomes:UP000002209};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00372};
KW   Histidine metabolism {ECO:0000256|HAMAP-Rule:MF_00372,
KW   ECO:0000256|SAAS:SAAS00325481};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00372,
KW   ECO:0000256|SAAS:SAAS00325474, ECO:0000313|EMBL:BAH38976.1};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00372, ECO:0000256|SAAS:SAAS00325485};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00372,
KW   ECO:0000256|SAAS:SAAS00325493};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002209};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00372, ECO:0000256|SAAS:SAAS00325492}.
FT   DOMAIN      117    395       Amidohydro_3. {ECO:0000259|Pfam:PF07969}.
FT   METAL        76     76       Zinc or iron. {ECO:0000256|HAMAP-Rule:
FT                                MF_00372}.
FT   METAL        78     78       Zinc or iron. {ECO:0000256|HAMAP-Rule:
FT                                MF_00372}.
FT   METAL       249    249       Zinc or iron. {ECO:0000256|HAMAP-Rule:
FT                                MF_00372}.
FT   METAL       324    324       Zinc or iron. {ECO:0000256|HAMAP-Rule:
FT                                MF_00372}.
FT   BINDING      85     85       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00372}.
FT   BINDING      98     98       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00372}.
FT   BINDING     148    148       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00372}.
FT   BINDING     181    181       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00372}.
FT   BINDING     252    252       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00372}.
SQ   SEQUENCE   416 AA;  44012 MW;  5E36C713A3FE7CC3 CRC64;
     MLFVNAAQTL TASGPARARR GHEMRDADVR SGVGVAVQGE RIVMVDTDDA LRRAFADATE
     VDCDRGLLAP GFVDSHTHTV FGAARYAEQE LRATGVPYLE IARRGGGIHS SVRDLRSRTN
     DELFALAVPR LARLASGGVT TVEIKSGYGL TVADELRTLR VIRDLATSQP LDIVATCLGA
     HEVPLEFRDR DGGRQEWLAL LAEELFPQVA AESLAQFADI FCEPGVFTVD EARVLLQHGQ
     RLGLRAKLHA DELHDGGAAG LAAELGAISA DHLAAISPEG IAALAASETV ATVLPATMLF
     LGTGRQAPAR QLIEAGAAVA LATDFNPGTS PLTAFPLVMT LAVSELRLSA SEAWIASTVN
     GAAALGLAGV TGQLSPGFRA DLAIHAVEDF RALPYWFGER LCVGSWSRGR ACHPMR
//
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