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Database: UniProt
Entry: E1X143_HALMS
LinkDB: E1X143_HALMS
Original site: E1X143_HALMS 
ID   E1X143_HALMS            Unreviewed;       506 AA.
AC   E1X143;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Succinylglutamic semialdehyde dehydrogenase {ECO:0000313|EMBL:CBW28113.1};
GN   Name=astD {ECO:0000313|EMBL:CBW28113.1};
GN   OrderedLocusNames=BMS_3370 {ECO:0000313|EMBL:CBW28113.1};
OS   Halobacteriovorax marinus (strain ATCC BAA-682 / DSM 15412 / SJ)
OS   (Bacteriovorax marinus).
OC   Bacteria; Bdellovibrionota; Bacteriovoracia; Bacteriovoracales;
OC   Halobacteriovoraceae; Halobacteriovorax.
OX   NCBI_TaxID=862908 {ECO:0000313|EMBL:CBW28113.1, ECO:0000313|Proteomes:UP000008963};
RN   [1] {ECO:0000313|Proteomes:UP000008963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-682 / DSM 15412 / SJ
RC   {ECO:0000313|Proteomes:UP000008963};
RX   PubMed=22955231; DOI=10.1038/ismej.2012.90;
RA   Crossman L.C., Chen H., Cerdeno-Tarraga A.M., Brooks K., Quail M.A.,
RA   Pineiro S.A., Hobley L., Sockett R.E., Bentley S.D., Parkhill J.,
RA   Williams H.N., Stine O.C.;
RT   "A small predatory core genome in the divergent marine Bacteriovorax
RT   marinus SJ and the terrestrial Bdellovibrio bacteriovorus.";
RL   ISME J. 7:148-160(2013).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; FQ312005; CBW28113.1; -; Genomic_DNA.
DR   RefSeq; WP_014245882.1; NC_016620.1.
DR   AlphaFoldDB; E1X143; -.
DR   STRING; 862908.BMS_3370; -.
DR   KEGG; bmx:BMS_3370; -.
DR   PATRIC; fig|862908.3.peg.3223; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_7; -.
DR   Proteomes; UP000008963; Chromosome.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
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; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008963}.
FT   DOMAIN          29..471
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        257
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   506 AA;  56308 MW;  572570480B194450 CRC64;
     MTYELKGNYF NNEFIQPPLT GPDAVEKWIT RTSPANSAQT LWKCPIHYGH AEEVVESATN
     GFKEWRKTSV QERVALLKKY QEELITKKEE IAKAISLEMG KPYWEALTEA GALIAKVDVT
     ISDSLPRVES KVYDEIMPMT NGYIHYKPIG PCFIIGPFNF PCHLANGQIT SALIAGNTII
     FKPSEKTCYS AQLMFECLSR AGFPKGVINL VQGDGEVARR ILKSKDIKAV FFTGSKDIGK
     SILKQTHEDL GKLVSLELGG KNPAIVHSDV NIDYVLGELV KGSFLTTGQR CTSTAIVPIH
     RSICDEVVSK FHELSKRIIV DHPIEHDEVP FMGPLVDQQA LDSYLLYVGM AKREGLEEIM
     RGKKLEKTFD GHYVSPSIHL AQKWDDKSHF LSSEIFGPNC TFIPYDDIEE AIEIANKTEY
     GLAASIFTKD HSLYELALRD LDHGYVNLNR STVGASAKLP FGGVKNSGNY HPAAVTTIDA
     CVYQQASLEI LKEEETDLNN IVGLKK
//
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