ASTE_VIBCH
ID ASTE_VIBCH Reviewed; 342 AA.
AC Q9KSL4;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=VC_1242;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of succinylglutamate desuccinylase from Vibrio cholerae,
RT Northeast structural genomics target Vcr20.";
RL Submitted (APR-2006) 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 Evidence={ECO:0000255|HAMAP-Rule:MF_00767};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00767};
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; AE003852; AAF94401.1; -; Genomic_DNA.
DR PIR; E82224; E82224.
DR RefSeq; NP_230887.1; NC_002505.1.
DR RefSeq; WP_000167426.1; NZ_LT906614.1.
DR PDB; 2G9D; X-ray; 3.00 A; A=1-342.
DR PDBsum; 2G9D; -.
DR AlphaFoldDB; Q9KSL4; -.
DR SMR; Q9KSL4; -.
DR STRING; 243277.VC_1242; -.
DR DNASU; 2614679; -.
DR EnsemblBacteria; AAF94401; AAF94401; VC_1242.
DR GeneID; 57739912; -.
DR KEGG; vch:VC_1242; -.
DR PATRIC; fig|243277.26.peg.1183; -.
DR eggNOG; COG2988; Bacteria.
DR HOGENOM; CLU_071608_0_0_6; -.
DR OMA; FIIAHPE; -.
DR BioCyc; VCHO:VC1242-MON; -.
DR UniPathway; UPA00185; UER00283.
DR EvolutionaryTrace; Q9KSL4; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Arginine metabolism; Hydrolase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..342
FT /note="Succinylglutamate desuccinylase"
FT /id="PRO_0000174650"
FT ACT_SITE 219
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT TURN 10..14
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:2G9D"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:2G9D"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2G9D"
FT HELIX 125..140
FT /evidence="ECO:0007829|PDB:2G9D"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:2G9D"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 149..159
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:2G9D"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:2G9D"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:2G9D"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:2G9D"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:2G9D"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 258..267
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 319..329
FT /evidence="ECO:0007829|PDB:2G9D"
FT STRAND 332..341
FT /evidence="ECO:0007829|PDB:2G9D"
SQ SEQUENCE 342 AA; 39093 MW; D5D646FA0F6E3796 CRC64;
MTKSLFRQSF LFDSLDLDHP MVAQTVRTEQ GVTLKLHQRG VLEVIPAQTD AATKNMVISC
GIHGDETAPM ELLDKWIDDI VSGFQPVAER CLFIMAHPQA TVRHVRFIEQ NLNRLFDDKP
HTPSTELAIA DNLKVLLRQF FANTDEHSRW HLDLHCAIRG SKHYSFAVSP KARHPVRSRS
LMQFIEQAHI EAVMLSNAPS STFSWYSAEH YAAQALTLEL GQVARLGENL LDRLLAFDLA
MRDLISRHKP EHLPRKSVMY RVSRTIVRLH DDFDFRFSDD VENFTAFMHG EVFGHDGDKP
LMAKNEGEAI VFPNRKVAIG QRAALMVCKV NTRYEDDQLV YD
