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Database: UniProt
Entry: A0A1M3D8Y5_9SPHN
LinkDB: A0A1M3D8Y5_9SPHN
Original site: A0A1M3D8Y5_9SPHN 
ID   A0A1M3D8Y5_9SPHN        Unreviewed;       470 AA.
AC   A0A1M3D8Y5;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Succinylglutamate-semialdehyde dehydrogenase {ECO:0000313|EMBL:OJV29322.1};
GN   ORFNames=BGO24_03660 {ECO:0000313|EMBL:OJV29322.1};
OS   Sphingomonas sp. 67-36.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1895849 {ECO:0000313|EMBL:OJV29322.1, ECO:0000313|Proteomes:UP000183964};
RN   [1] {ECO:0000313|EMBL:OJV29322.1, ECO:0000313|Proteomes:UP000183964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=67-36 {ECO:0000313|EMBL:OJV29322.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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:OJV29322.1}.
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DR   EMBL; MKSU01000022; OJV29322.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3D8Y5; -.
DR   STRING; 1895849.BGO24_03660; -.
DR   Proteomes; UP000183964; Unassembled WGS sequence.
DR   GO; GO:0043824; F:succinylglutamate-semialdehyde dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   CDD; cd07095; ALDH_SGSD_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};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345}.
FT   DOMAIN          19..445
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        229
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   470 AA;  50399 MW;  9FC08072479BCD44 CRC64;
     MATELVSFEP ASGAELWRGA ISDVDAEVAA ARGGWASWAA RALTVRIETL RRFANVVRAR
     ADAFADLIAR ETGKPLWEAR TEVDSVIAKV DISVSAYAER TAQRRLDSPM GSRMALRHKP
     HGVLAVLGPY NFPAHLPNGH IVPALIAGNA VVFKPSEKTP ATGAFLVDCL REAGVPENCI
     RLVIGGPDEG KALAAHDGID GLLFTGSART GLALNRAFAE KPEKILALEM GGNNPIVVWD
     TPDLWQAAVL VAQSAFTTAG QRCTAARRLI VEEKLFDPLI EELGKLIARL VVDEPFANPA
     PFMGPVIDND AADQLAESFL ALLMKGGRPI RHLERPDPAR PFLLPALIDV TGVRERPDTE
     LFGPILQVSR CSDFDAAIAE ANDTRYGLSA SLISQTPQLF DRFWARARAG IVNWNKPTNG
     ASSSAPFGGI GWSGNHRPSA YYAADYCAYP VVSNEADAAR ATIGIGLRDG
//
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