ID K6XWK8_9ALTE Unreviewed; 490 AA.
AC K6XWK8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
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:GAC16046.1};
GN ORFNames=GLIP_3432 {ECO:0000313|EMBL:GAC16046.1};
OS Aliiglaciecola lipolytica E3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Aliiglaciecola.
OX NCBI_TaxID=1127673 {ECO:0000313|EMBL:GAC16046.1, ECO:0000313|Proteomes:UP000006334};
RN [1] {ECO:0000313|EMBL:GAC16046.1, ECO:0000313|Proteomes:UP000006334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:GAC16046.1,
RC ECO:0000313|Proteomes:UP000006334};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC16046.1}.
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DR EMBL; BAEN01000065; GAC16046.1; -; Genomic_DNA.
DR RefSeq; WP_008845849.1; NZ_BAEN01000065.1.
DR AlphaFoldDB; K6XWK8; -.
DR STRING; 1127673.GLIP_3432; -.
DR eggNOG; COG1012; Bacteria.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00185; UER00282.
DR Proteomes; UP000006334; 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:UP000006334}.
FT DOMAIN 15..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 490 AA; 52710 MW; BFB2F8BC71AEF46E CRC64;
MTTQAHYIAG EWHLGEGHDI QSIDPAKNKV IWQAKSASPK QIDAAVKAAR NAFLAWSDLT
FENRLQIVKK YAELLGENKQ DLAQTIAQET GKPLWETATE VGAMVGKIAI SERAYHDRTG
TVENPMPVGK AFIRHKPHGV VAVFGPYNFP GHLPNGHIVP ALLAGNTIVF KPSDLTPLVA
EKMVKIWQQA GLPAGVINLV QGEVETGKAL ASHTGIDGLF FTGSSRTGKI LHEQFAGHPG
KILALEMGGN NPLIVKDAKD IDAVVHDIVQ SAFVTSGQRC TCARRLFIQQ NAQGDAILAK
LIDVTKNIKV DQYDAEEQPF MGAMISANAA AGMVRAQQQL VELGATPLVE LKHLDTNTGF
VTPGILDVTS MADKMPDEEH FGPLLKVIRY TDFDQAIASA NNTNFGLSAG FIGDSESDYQ
HFFKRIRAGI VNWNRPITGA SSAAPFGGIG ESGNHRASAY YAADYCAFPV ASVELEQVTL
PASLSPGLTL
//
