ID A0A0F4NMZ1_9VIBR Unreviewed; 485 AA.
AC A0A0F4NMZ1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
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:KJY84218.1};
GN ORFNames=TW81_05340 {ECO:0000313|EMBL:KJY84218.1};
OS Vibrio galatheae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=579748 {ECO:0000313|EMBL:KJY84218.1, ECO:0000313|Proteomes:UP000033673};
RN [1] {ECO:0000313|EMBL:KJY84218.1, ECO:0000313|Proteomes:UP000033673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2757 {ECO:0000313|EMBL:KJY84218.1,
RC ECO:0000313|Proteomes:UP000033673};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KJY84218.1}.
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DR EMBL; JXXV01000011; KJY84218.1; -; Genomic_DNA.
DR RefSeq; WP_045954685.1; NZ_JXXV01000011.1.
DR AlphaFoldDB; A0A0F4NMZ1; -.
DR STRING; 579748.TW81_05340; -.
DR PATRIC; fig|579748.3.peg.1093; -.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00185; UER00282.
DR Proteomes; UP000033673; 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:UP000033673}.
FT DOMAIN 9..458
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 243
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01174,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 278
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01174"
FT BINDING 220..225
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01174"
SQ SEQUENCE 485 AA; 51698 MW; 53BC9936B9CAB600 CRC64;
MTHWIAGEWV AGQGEPMNSI SPYNNEVIWQ GESATPEQVE QAVSAARSAF VSWKKMSFAQ
REAVVVAFAE KVKQNSEQIA EIIAKETGKP IWETRTEAAA MAGKIAISIR AYHDRTGEAQ
REAAGNQIVL RHRPLGVMAV FGPYNFPGHL PNGHIVPALL AGNTVVFKPS EQTPLTGEFA
MKLWEQAGLP KGVINLVQGA KETGIALADS KGLDGVLFTG SANTGHILHK QFAGQPGKML
ALEMGGNNPM VISDNYGDVD ATVYTIIQSA FISAGQRCTC ARRLYVPVGE KGDQLVSKLV
EATNKIRVDQ PFAEPAPFMG PQISKAAADF ILAAQANLHN LGGVSLVEAK AGEAAFVTPG
IIDVTAIAEL PDEEYFGPLL QLVRYQGLEQ AVELANDTRF GLSAGLVSTD DGEWEYFVDH
IRAGIVNRNR QLTGASGDAP FGGPGASGNL RPSAYYAADY CAYPMASMEG GETELPATLS
PGVEL
//
