ASTD_BURTA
ID ASTD_BURTA Reviewed; 487 AA.
AC Q2SXN9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=N-succinylglutamate 5-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01174};
DE EC=1.2.1.71 {ECO:0000255|HAMAP-Rule:MF_01174};
DE AltName: Full=Succinylglutamic semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01174};
DE Short=SGSD {ECO:0000255|HAMAP-Rule:MF_01174};
GN Name=astD {ECO:0000255|HAMAP-Rule:MF_01174}; OrderedLocusNames=BTH_I1778;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
CC -!- FUNCTION: Catalyzes the NAD-dependent reduction of succinylglutamate
CC semialdehyde into succinylglutamate. {ECO:0000255|HAMAP-Rule:MF_01174}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01174};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC pathway; L-glutamate and succinate from L-arginine: step 4/5.
CC {ECO:0000255|HAMAP-Rule:MF_01174}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. AstD
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01174}.
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DR EMBL; CP000086; ABC38809.1; -; Genomic_DNA.
DR RefSeq; WP_009890066.1; NZ_CP008785.1.
DR PDB; 4KNA; X-ray; 1.95 A; A/B=1-487.
DR PDBsum; 4KNA; -.
DR AlphaFoldDB; Q2SXN9; -.
DR SMR; Q2SXN9; -.
DR PRIDE; Q2SXN9; -.
DR EnsemblBacteria; ABC38809; ABC38809; BTH_I1778.
DR KEGG; bte:BTH_I1778; -.
DR HOGENOM; CLU_005391_1_0_4; -.
DR OMA; NWNKQLT; -.
DR OrthoDB; 744602at2; -.
DR UniPathway; UPA00185; UER00282.
DR Proteomes; UP000001930; Chromosome I.
DR GO; GO:0043824; F:succinylglutamate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
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.
FT CHAIN 1..487
FT /note="N-succinylglutamate 5-semialdehyde dehydrogenase"
FT /id="PRO_0000262392"
FT ACT_SITE 244
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT ACT_SITE 278
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT BINDING 221..226
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:4KNA"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:4KNA"
FT HELIX 37..56
FT /evidence="ECO:0007829|PDB:4KNA"
FT HELIX 59..75
FT /evidence="ECO:0007829|PDB:4KNA"
FT HELIX 77..88
FT /evidence="ECO:0007829|PDB:4KNA"
FT HELIX 92..116
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:4KNA"
FT HELIX 150..162
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:4KNA"
FT HELIX 175..187
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:4KNA"
FT HELIX 202..209
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:4KNA"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:4KNA"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:4KNA"
FT HELIX 259..271
FT /evidence="ECO:0007829|PDB:4KNA"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 281..289
FT /evidence="ECO:0007829|PDB:4KNA"
FT HELIX 290..304
FT /evidence="ECO:0007829|PDB:4KNA"
FT HELIX 325..340
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 379..389
FT /evidence="ECO:0007829|PDB:4KNA"
FT HELIX 390..397
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 404..409
FT /evidence="ECO:0007829|PDB:4KNA"
FT HELIX 413..422
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 426..432
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:4KNA"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:4KNA"
FT HELIX 459..463
FT /evidence="ECO:0007829|PDB:4KNA"
FT STRAND 464..471
FT /evidence="ECO:0007829|PDB:4KNA"
SQ SEQUENCE 487 AA; 51722 MW; C403DA2B5E20965E CRC64;
MTELFIDGAW VDGAGPVFAS RNPGTNERVW EGASASADDV ERAVASARRA FAAWSALDLD
ARCTIVKRFA ALLVERKEAL ATMIGRETGK PLWEARTEVA SMAAKVDISI TAYHERTGEK
RAPMADGVAV LRHRPHGVVA VFGPYNFPGH LPNGHIVPAL IAGNTVVFKP SELAPGVARA
TVEIWRDAGL PAGVLNLVQG EKDTGVALAN HRQIDGLFFT GSSDTGTLLH KQFGGRPEIV
LALEMGGNNP LVVAEVEDID AAVHHAIQSA FLSAGQRCTC ARRILVPRGA FGDRFVARLA
DVASKITASV FDADPQPFMG AVISARAASR LVAAQARLVG LGASPIIEMK QRDPALGFVN
AAILDVTNVR ELPDEEHFGP LAQIVRYTDL DDAIARANDT AFGLSAGLLA DDEQAWHTFR
RAIRAGIVNW NRPTNGASSA APFGGAGRSG NHRPSAYYAA DYCAYPMASV ESAQLQMPAS
LSPGLHF
