ENA_EUBBA
ID ENA_EUBBA Reviewed; 386 AA.
AC Q0QLE9;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Enamidase {ECO:0000312|EMBL:ABC88401.1};
DE EC=3.5.2.18;
GN Name=Ena {ECO:0000312|EMBL:ABC88401.1};
OS Eubacterium barkeri (Clostridium barkeri).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1528;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABC88401.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-28; 45-68 AND
RP 271-290, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, SUBUNIT, AND MASS SPECTROMETRY.
RC STRAIN=ATCC 25849 / DSM 1223 / JCM 1389 / NCIMB 10623 / VKM B-1775 / VPI
RC 5359 {ECO:0000312|EMBL:ABC88401.1};
RX PubMed=16894175; DOI=10.1073/pnas.0601635103;
RA Alhapel A., Darley D.J., Wagener N., Eckel E., Elsner N., Pierik A.J.;
RT "Molecular and functional analysis of nicotinate catabolism in Eubacterium
RT barkeri.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12341-12346(2006).
RN [2] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH IRON AND ZINC,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 25849 / DSM 1223 / JCM 1389 / NCIMB 10623 / VKM B-1775 / VPI
RC 5359 {ECO:0000269|PubMed:18805424};
RX PubMed=18805424; DOI=10.1016/j.jmb.2008.09.002;
RA Kress D., Alhapel A., Pierik A.J., Essen L.O.;
RT "The crystal structure of enamidase: a bifunctional enzyme of the
RT nicotinate catabolism.";
RL J. Mol. Biol. 384:837-847(2008).
CC -!- FUNCTION: Decyclization of 6-oxo-1,4,5,6-tetrahydronicotinate to form
CC 2-(enamine)glutarate, followed by hydrolysis to form (S)-2-
CC formylglutarate. {ECO:0000269|PubMed:16894175,
CC ECO:0000269|PubMed:18805424}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,4,5,6-tetrahydro-6-oxonicotinate + 2 H2O = 2-formylglutarate
CC + NH4(+); Xref=Rhea:RHEA:17209, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57777, ChEBI:CHEBI:58776; EC=3.5.2.18;
CC Evidence={ECO:0000269|PubMed:16894175, ECO:0000269|PubMed:18805424};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Note=Binds 1 Fe cation per subunit.;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 mM for 6-oxo-1,4,5,6-tetrahydronicotinate
CC {ECO:0000269|PubMed:16894175};
CC -!- PATHWAY: Cofactor degradation; nicotinate degradation; propanoate and
CC pyruvate from 6-hydroxynicotinate: step 2/8.
CC {ECO:0000269|PubMed:16894175}.
CC -!- SUBUNIT: Homotetramer. Dimer of dimers. {ECO:0000269|PubMed:16894175,
CC ECO:0000269|PubMed:18805424}.
CC -!- MASS SPECTROMETRY: Mass=39750; Mass_error=40; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16894175};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenine deaminase family. {ECO:0000305}.
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DR EMBL; DQ310789; ABC88401.1; -; Genomic_DNA.
DR PDB; 2VUN; X-ray; 1.89 A; A/B/C/D=1-386.
DR PDBsum; 2VUN; -.
DR AlphaFoldDB; Q0QLE9; -.
DR SMR; Q0QLE9; -.
DR DIP; DIP-61252N; -.
DR STRING; 1528.SAMN04488579_11211; -.
DR KEGG; ag:ABC88401; -.
DR BioCyc; MetaCyc:MON-13673; -.
DR BRENDA; 3.5.2.18; 1459.
DR SABIO-RK; Q0QLE9; -.
DR UniPathway; UPA01010; UER01013.
DR EvolutionaryTrace; Q0QLE9; -.
DR GO; GO:0043792; F:enamidase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901848; P:nicotinate catabolic process; IDA:UniProtKB.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Iron; Metal-binding;
KW Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16894175"
FT CHAIN 2..386
FT /note="Enamidase"
FT /evidence="ECO:0000269|PubMed:16894175"
FT /id="PRO_0000403998"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:18805424"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:18805424"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:18805424"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:18805424"
FT BINDING 193
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:18805424"
FT BINDING 220
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:18805424"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:18805424"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:2VUN"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:2VUN"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2VUN"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:2VUN"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:2VUN"
FT HELIX 111..127
FT /evidence="ECO:0007829|PDB:2VUN"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2VUN"
FT HELIX 148..156
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:2VUN"
FT HELIX 173..185
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:2VUN"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:2VUN"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:2VUN"
FT HELIX 230..239
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:2VUN"
FT HELIX 252..265
FT /evidence="ECO:0007829|PDB:2VUN"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:2VUN"
FT HELIX 287..298
FT /evidence="ECO:0007829|PDB:2VUN"
FT HELIX 303..310
FT /evidence="ECO:0007829|PDB:2VUN"
FT HELIX 312..318
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:2VUN"
FT HELIX 347..353
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 367..372
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:2VUN"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:2VUN"
SQ SEQUENCE 386 AA; 39923 MW; 84AF39771B54B87D CRC64;
MSKTIIKNIG KIVSGDIKSP VLQADTIVVE DGLIAAIGGE ELMKDAGDAT IIDAAGSTVT
PGLLDTHVHV SGGDYAPRQK TMDFISSALH GGVTTMISAG SPHFPGRPKD AAGTKALAIT
LSKSYYNARP AGVKVHGGAV ILEKGLTEED FIEMKKEGVW IVGEVGLGTI KNPEDAAPMV
EWAHKHGFKV QMHTGGTSIP GSSTVTADDV IKTKPDVVSH INGGPTAISV QEVDRIMDET
DFAMEIVQCG NPKIADYVAR RAAEKGQLGR VIFGNDAPSG TGLIPLGILR NMCQIASMSD
IDPEVAVCMA TGNSTAVYGL NTGVIAPGKE ADLIIMDTPL GSVAEDAMGA IAAGDIPGIS
VVLIDGEAVV TKSRNTPPAK RAAKIL
