ASTD_PSEAE
ID ASTD_PSEAE Reviewed; 487 AA.
AC O50174;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=N-succinylglutamate 5-semialdehyde dehydrogenase;
DE EC=1.2.1.71;
DE AltName: Full=Succinylglutamic semialdehyde dehydrogenase;
DE Short=SGSD;
GN Name=astD; Synonyms=aruD; OrderedLocusNames=PA0898;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9393691; DOI=10.1128/jb.179.23.7280-7290.1997;
RA Itoh Y.;
RT "Cloning and characterization of the aru genes encoding enzymes of the
RT catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa.";
RL J. Bacteriol. 179:7280-7290(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Catalyzes the NAD-dependent reduction of succinylglutamate
CC semialdehyde into succinylglutamate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-succinyl-L-glutamate 5-semialdehyde + NAD(+) = 2 H(+)
CC + N-succinyl-L-glutamate + NADH; Xref=Rhea:RHEA:10812,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58520, ChEBI:CHEBI:58763; EC=1.2.1.71;
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC pathway; L-glutamate and succinate from L-arginine: step 4/5.
CC {ECO:0000269|PubMed:9393691}.
CC -!- INDUCTION: By arginine, under the control of ArgR.
CC {ECO:0000269|PubMed:9393691}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. AstD
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC46012.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG04287.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF011922; AAC46012.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE004091; AAG04287.1; ALT_INIT; Genomic_DNA.
DR PIR; C83533; C83533.
DR RefSeq; NP_249589.1; NC_002516.2.
DR PDB; 3JU8; X-ray; 1.82 A; A/B=1-486.
DR PDBsum; 3JU8; -.
DR AlphaFoldDB; O50174; -.
DR SMR; O50174; -.
DR STRING; 287.DR97_1045; -.
DR PaxDb; O50174; -.
DR PRIDE; O50174; -.
DR EnsemblBacteria; AAG04287; AAG04287; PA0898.
DR GeneID; 883040; -.
DR KEGG; pae:PA0898; -.
DR PATRIC; fig|208964.12.peg.933; -.
DR PseudoCAP; PA0898; -.
DR HOGENOM; CLU_005391_1_0_6; -.
DR InParanoid; O50174; -.
DR OMA; NWNKQLT; -.
DR PhylomeDB; O50174; -.
DR UniPathway; UPA00185; UER00282.
DR EvolutionaryTrace; O50174; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0043824; F:succinylglutamate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006527; P:arginine catabolic process; IDA:PseudoCAP.
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; cd07095; ALDH_SGSD_AstD; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR HAMAP; MF_01174; Aldedh_AstD; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR017649; SuccinylGlu_semiald_DH_AstD.
DR PANTHER; PTHR11699:SF197; PTHR11699:SF197; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR03240; arg_catab_astD; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Arginine metabolism; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..487
FT /note="N-succinylglutamate 5-semialdehyde dehydrogenase"
FT /id="PRO_0000056570"
FT ACT_SITE 244
FT /evidence="ECO:0000250"
FT ACT_SITE 278
FT /evidence="ECO:0000250"
FT BINDING 221..226
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:3JU8"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:3JU8"
FT HELIX 37..56
FT /evidence="ECO:0007829|PDB:3JU8"
FT HELIX 59..75
FT /evidence="ECO:0007829|PDB:3JU8"
FT HELIX 77..88
FT /evidence="ECO:0007829|PDB:3JU8"
FT HELIX 92..116
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3JU8"
FT HELIX 150..162
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:3JU8"
FT HELIX 175..187
FT /evidence="ECO:0007829|PDB:3JU8"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:3JU8"
FT HELIX 202..209
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:3JU8"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:3JU8"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:3JU8"
FT HELIX 259..271
FT /evidence="ECO:0007829|PDB:3JU8"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 280..289
FT /evidence="ECO:0007829|PDB:3JU8"
FT HELIX 290..305
FT /evidence="ECO:0007829|PDB:3JU8"
FT HELIX 325..340
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 379..389
FT /evidence="ECO:0007829|PDB:3JU8"
FT HELIX 390..398
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 404..409
FT /evidence="ECO:0007829|PDB:3JU8"
FT HELIX 413..422
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 425..432
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:3JU8"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:3JU8"
FT HELIX 459..463
FT /evidence="ECO:0007829|PDB:3JU8"
FT STRAND 464..471
FT /evidence="ECO:0007829|PDB:3JU8"
SQ SEQUENCE 487 AA; 51380 MW; 79EA94BF49476DFD CRC64;
MSTHYIAGQW LAGQGETLES LDPVGQGVVW SGRGADATQV DAAVCAAREA FPAWARRPLE
QRIELLERFA ATLKSRADEL ARVIGEETGK PLWESATEVT SMVNKVAISV QAFRERTGEK
SGPLADATAV LRHKPHGVVA VFGPYNFPGH LPNGHIVPAL LAGNCVVFKP SELTPKVAEL
TLKAWIQAGL PAGVLNLVQG GRETGVALAA HRGLDGLFFT GSSRTGNLLH SQFGGQPQKI
LALEMGGNNP LVVEEVADLD AAVYTIIQSA FISAGQRCTC ARRLLVPQGA WGDALLARLV
AVSATLRVGR FDEQPAPFMG AVISLSAAEH LLKAQEHLIG KGAQPLLAMT QPIDGAALLT
PGILDVSAVA ERPDEEFFGP LLQVIRYSDF AAAIREANAT QYGLAAGLLS DSRERFEQFL
VESRAGIVNW NKQLTGAASS APFGGIGASG NHRPSAYYAA DYCAYPVASL ESPSVSLPAT
LTPGISL
