ASTD_MARN8
ID ASTD_MARN8 Reviewed; 491 AA.
AC A1U5W8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=Maqu_3316;
OS Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS aquaeolei).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=351348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX PubMed=21335390; DOI=10.1128/aem.01866-10;
RA Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA Edwards K.J.;
RT "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT 'opportunitroph'.";
RL Appl. Environ. Microbiol. 77:2763-2771(2011).
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; CP000514; ABM20387.1; -; Genomic_DNA.
DR RefSeq; WP_011786728.1; NC_008740.1.
DR PDB; 5U0L; X-ray; 2.29 A; A/B=2-491.
DR PDB; 5U0M; X-ray; 3.08 A; A/B=2-491.
DR PDBsum; 5U0L; -.
DR PDBsum; 5U0M; -.
DR AlphaFoldDB; A1U5W8; -.
DR SMR; A1U5W8; -.
DR STRING; 351348.Maqu_3316; -.
DR EnsemblBacteria; ABM20387; ABM20387; Maqu_3316.
DR KEGG; maq:Maqu_3316; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_0_6; -.
DR OMA; NWNKQLT; -.
DR OrthoDB; 744602at2; -.
DR UniPathway; UPA00185; UER00282.
DR Proteomes; UP000000998; Chromosome.
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..491
FT /note="N-succinylglutamate 5-semialdehyde dehydrogenase"
FT /id="PRO_1000138051"
FT ACT_SITE 248
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT ACT_SITE 282
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT BINDING 225..230
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:5U0L"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:5U0L"
FT HELIX 41..58
FT /evidence="ECO:0007829|PDB:5U0L"
FT HELIX 63..79
FT /evidence="ECO:0007829|PDB:5U0L"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:5U0L"
FT HELIX 96..120
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:5U0L"
FT HELIX 154..165
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:5U0L"
FT HELIX 179..191
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:5U0L"
FT HELIX 206..213
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:5U0L"
FT HELIX 227..236
FT /evidence="ECO:0007829|PDB:5U0L"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:5U0L"
FT HELIX 263..275
FT /evidence="ECO:0007829|PDB:5U0L"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 285..293
FT /evidence="ECO:0007829|PDB:5U0L"
FT HELIX 294..307
FT /evidence="ECO:0007829|PDB:5U0L"
FT HELIX 329..344
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 382..392
FT /evidence="ECO:0007829|PDB:5U0L"
FT HELIX 393..400
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 407..412
FT /evidence="ECO:0007829|PDB:5U0L"
FT HELIX 416..425
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:5U0M"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:5U0L"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:5U0L"
FT HELIX 462..466
FT /evidence="ECO:0007829|PDB:5U0L"
FT STRAND 467..474
FT /evidence="ECO:0007829|PDB:5U0L"
SQ SEQUENCE 491 AA; 52483 MW; 52F36E678DD2AED1 CRC64;
MANLTGNVYI DGLWLPGHGA PFESVQPVTG ETVWDGNAAS LEDVDAAVRE ARKAFLAWRR
KSLAERQAVI EAFGELLEAN KEELAHQIGL ETGKPLWESR TEVAAMMGKI PISVKAYNER
TGHTESDVAG GHAVLRHRPH GVVAVFGPYN FPGHLPNGHI VPALLAGNTV VFKPSELTPG
VAELTVRLWE KAGLPDGVIN LVQGGSDTGK CLARHSLIDG LFFTGSSTVG HLLHEQFGGQ
PEKILALEMG GNNPLIVQNV SDLDGAVHHA LQSAFLSAGQ RCTCARRLLV PKGKKGDEFL
ARLVEVAARI TVAEFDADPQ PFMGSVISAE AANQLLKAQA AMLEKGATSL LEMKQLKPDT
GLLSPGIVDA TGIELEDQEF FGPLLTVYRY KGFDEALELA NNTRYGLSAG ILSDDRKLYN
RLVEEVRAGI VNWNRPLTGA SSAAPFGGVG ASGNHRPSAY YAADYCAWPM ASLEAGKSEL
PDSLAPGLNF D
