ID A0A432Z750_9GAMM Unreviewed; 489 AA.
AC A0A432Z750;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=N-succinylglutamate 5-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01174};
DE EC=1.2.1.71 {ECO:0000256|HAMAP-Rule:MF_01174};
DE AltName: Full=Succinylglutamic semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01174};
DE Short=SGSD {ECO:0000256|HAMAP-Rule:MF_01174};
GN Name=astD {ECO:0000256|HAMAP-Rule:MF_01174,
GN ECO:0000313|EMBL:RUO73734.1};
GN ORFNames=CWI81_11975 {ECO:0000313|EMBL:RUO73734.1};
OS Idiomarina seosinensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=281739 {ECO:0000313|EMBL:RUO73734.1, ECO:0000313|Proteomes:UP000287908};
RN [1] {ECO:0000313|EMBL:RUO73734.1, ECO:0000313|Proteomes:UP000287908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL-SP19 {ECO:0000313|EMBL:RUO73734.1,
RC ECO:0000313|Proteomes:UP000287908};
RX PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA Liu Y., Lai Q., Shao Z.;
RT "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT Idiomarinaceae.";
RL Front. Microbiol. 9:2453-2453(2018).
CC -!- FUNCTION: Catalyzes the NAD-dependent reduction of succinylglutamate
CC semialdehyde into succinylglutamate. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01174}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. AstD
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01174}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RUO73734.1}.
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DR EMBL; PIQF01000004; RUO73734.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432Z750; -.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00185; UER00282.
DR Proteomes; UP000287908; Unassembled WGS sequence.
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 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 NCBIfam; TIGR03240; arg_catab_astD; 1.
DR PANTHER; PTHR11699:SF228; 4-TRIMETHYLAMINOBUTYRALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Arginine metabolism {ECO:0000256|ARBA:ARBA00022503, ECO:0000256|HAMAP-
KW Rule:MF_01174};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01174};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01174}; Reference proteome {ECO:0000313|Proteomes:UP000287908}.
FT DOMAIN 12..464
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 246
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01174,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 280
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01174"
FT BINDING 223..228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01174"
SQ SEQUENCE 489 AA; 52707 MW; E5EC6EFF0AC365E2 CRC64;
MSSSVQFIDG CWSAGNGKTF KSIDPARNQP VWSGAAADDN QVDAAVMAAR KAFPEWSQRS
LEERLAICKR FSELLAENKE ELAQTMAEET GKPVWETRTE VGAMVGKVAI SERAYNERTG
TVENDMPGAK AFIRHKPHGV VAVYGPYNFP GHLPNGHIVP ALIAGNTVVF KPSELTPKVA
ELTVKLWEKA GIPAGVLNLV QGEVETGKAL SAHPQIDGLY FTGSSNTGHL LHKQFGGRPD
KILALEMGGN NPLVVTNVSD IDATVHNIVQ SAYITSGQRC TCARRLFIED TEQGRAVLDR
LVEVTKNIEV GDYEAEPQPF MGAMISAQAA AGMADAQSEL LRLGGKSLVK LVHEDPKTGL
VTPGIVDVTD VEDIPDEEYF GPLLKVYRFT SLDEAIAEAN NTRYGLSAGI LCDDEETYRY
FFKHIRAGIV NWNKPITGAS SAAPFGGIGA SGNHRASAYY AADYCSYPVA SVEADSMSLP
ESLAPGLKF
//
