ASTE_CHRVO
ID ASTE_CHRVO Reviewed; 333 AA.
AC Q7NU26;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Succinylglutamate desuccinylase {ECO:0000255|HAMAP-Rule:MF_00767};
DE EC=3.5.1.96 {ECO:0000255|HAMAP-Rule:MF_00767};
GN Name=astE {ECO:0000255|HAMAP-Rule:MF_00767}; OrderedLocusNames=CV_2877;
OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS 12614 / NCIMB 9131 / NCTC 9757).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=243365;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
RX PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S.,
RA Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M.,
RA Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P.,
RA Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S.,
RA Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N.,
RA Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P.,
RA Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z.,
RA de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F.,
RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C.,
RA Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M.,
RA Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT "The complete genome sequence of Chromobacterium violaceum reveals
RT remarkable and exploitable bacterial adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS.
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of the succinylglutamate desuccinylase from
RT Chromobacterium violaceum, Northeast structural genomics target Cvr22.";
RL Submitted (MAY-2005) to the PDB data bank.
CC -!- FUNCTION: Transforms N(2)-succinylglutamate into succinate and
CC glutamate. {ECO:0000255|HAMAP-Rule:MF_00767}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-succinyl-L-glutamate = L-glutamate + succinate;
CC Xref=Rhea:RHEA:15169, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:58763; EC=3.5.1.96;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00767};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC pathway; L-glutamate and succinate from L-arginine: step 5/5.
CC {ECO:0000255|HAMAP-Rule:MF_00767}.
CC -!- SIMILARITY: Belongs to the AspA/AstE family. Succinylglutamate
CC desuccinylase subfamily. {ECO:0000255|HAMAP-Rule:MF_00767}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016825; AAQ60545.1; -; Genomic_DNA.
DR RefSeq; WP_011136424.1; NC_005085.1.
DR PDB; 1YW4; X-ray; 2.00 A; A/B=1-333.
DR PDBsum; 1YW4; -.
DR AlphaFoldDB; Q7NU26; -.
DR SMR; Q7NU26; -.
DR STRING; 243365.CV_2877; -.
DR EnsemblBacteria; AAQ60545; AAQ60545; CV_2877.
DR KEGG; cvi:CV_2877; -.
DR eggNOG; COG2988; Bacteria.
DR HOGENOM; CLU_071608_0_0_4; -.
DR OMA; KRYLHSD; -.
DR OrthoDB; 632656at2; -.
DR UniPathway; UPA00185; UER00283.
DR EvolutionaryTrace; Q7NU26; -.
DR Proteomes; UP000001424; Chromosome.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProtKB-UniRule.
DR GO; GO:0009017; F:succinylglutamate desuccinylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:UniProtKB-UniRule.
DR GO; GO:0019545; P:arginine catabolic process to succinate; IEA:UniProtKB-UniPathway.
DR CDD; cd03855; M14_ASTE; 1.
DR HAMAP; MF_00767; Arg_catab_AstE; 1.
DR InterPro; IPR007036; Aste_AspA.
DR InterPro; IPR016681; SuccinylGlu_desuccinylase.
DR Pfam; PF04952; AstE_AspA; 1.
DR PIRSF; PIRSF017020; AstE; 1.
DR TIGRFAMs; TIGR03242; arg_catab_astE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Arginine metabolism; Hydrolase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..333
FT /note="Succinylglutamate desuccinylase"
FT /id="PRO_0000174638"
FT ACT_SITE 214
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:1YW4"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:1YW4"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1YW4"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:1YW4"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:1YW4"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:1YW4"
FT HELIX 61..74
FT /evidence="ECO:0007829|PDB:1YW4"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:1YW4"
FT HELIX 91..96
FT /evidence="ECO:0007829|PDB:1YW4"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1YW4"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1YW4"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1YW4"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:1YW4"
FT HELIX 120..137
FT /evidence="ECO:0007829|PDB:1YW4"
FT STRAND 143..153
FT /evidence="ECO:0007829|PDB:1YW4"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:1YW4"
FT HELIX 174..181
FT /evidence="ECO:0007829|PDB:1YW4"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:1YW4"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:1YW4"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:1YW4"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:1YW4"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:1YW4"
FT HELIX 230..241
FT /evidence="ECO:0007829|PDB:1YW4"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:1YW4"
FT STRAND 257..265
FT /evidence="ECO:0007829|PDB:1YW4"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:1YW4"
FT STRAND 317..328
FT /evidence="ECO:0007829|PDB:1YW4"
SQ SEQUENCE 333 AA; 36520 MW; EE3CD3D2F4C1AA9C CRC64;
MTHSPSFLQH ALSSSDTRAE WPLPGGLAAR WLAPGCVELN GDARGADSVL LSCGVHGNET
APIEVVDGML TDIAAGQLAL NCRLLVMFAN LDAIRQGVRY GNYDMNRLFN GAHARHPELP
ESVRAAELET LAAEFFAGAR ARKLHYDLHT AIRGSVFEKF AIYPFLHDGR THKREQLAWL
QRCGIEAVLL HTQPANTFSY FTSQYCEADA FTLELGKARP FGQNDLSRFS GIDGALRGLL
SNPQANVPDL DEDKLPLFRA KYDLVKHSEA FKLNLADSVE NFTLLPDGML IAEDGAVRYQ
ATGGEERILF PNPAVKPGLR AGIVVEPARL PSR
