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Database: UniProt
Entry: A0A3D9BX47_9RHOB
LinkDB: A0A3D9BX47_9RHOB
Original site: A0A3D9BX47_9RHOB 
ID   A0A3D9BX47_9RHOB        Unreviewed;       491 AA.
AC   A0A3D9BX47;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=NAD-dependent succinate-semialdehyde dehydrogenase {ECO:0000313|EMBL:REC57941.1};
GN   ORFNames=DRV84_04985 {ECO:0000313|EMBL:REC57941.1};
OS   Rhodosalinus sediminis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodosalinus.
OX   NCBI_TaxID=1940533 {ECO:0000313|EMBL:REC57941.1, ECO:0000313|Proteomes:UP000257131};
RN   [1] {ECO:0000313|EMBL:REC57941.1, ECO:0000313|Proteomes:UP000257131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WDN1C137 {ECO:0000313|EMBL:REC57941.1,
RC   ECO:0000313|Proteomes:UP000257131};
RX   PubMed=29043957; DOI=10.1099/ijsem.0.002424;
RA   Guo L.Y., Ling S.K., Li C.M., Chen G.J., Du Z.J.;
RT   "Rhodosalinus sediminis gen. nov., sp. nov., isolated from marine
RT   saltern.";
RL   Int. J. Syst. Evol. Microbiol. 67:5108-5113(2017).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, 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:REC57941.1}.
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DR   EMBL; QOHR01000004; REC57941.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D9BX47; -.
DR   OrthoDB; 9812625at2; -.
DR   Proteomes; UP000257131; Unassembled WGS sequence.
DR   GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro.
DR   GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IEA:InterPro.
DR   CDD; cd07103; ALDH_F5_SSADH_GabD; 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; IPR010102; Succ_semiAld_DH.
DR   NCBIfam; TIGR01780; SSADH; 1.
DR   PANTHER; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43353:SF5; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257131}.
FT   DOMAIN          29..487
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   491 AA;  52020 MW;  FDBBB36C401D7CCA CRC64;
     MLDQTTNLGS RLKDPALLEE RAFVAGAFAE GEGGTFEVTN PARGDVIARV ADCSRAQVAR
     AIDAAAAAQR DWAARTGKAR AAVLRRWFEL MMEHQEDLAV IMTAEQGKPL AESRGEIAYA
     AGFIEFSGEE AKRIYGETIP GHQRDKRITV IRQPVGVAAS ITPWNFPAAM ITRKAGPALA
     AGCAFVARPA SETPLSATAL AVLAERAGVP AGVFSVVPSG RASEIGREFC ENPTVRKLTF
     TGSTEVGRLL LRQAADQVKK CSMELGGNAP FLVFDDADLD AAVEGAIASK FRNNGQTCVC
     ANRIYVQSGV HDAFAEKLAA RVAELRVGDG LEEGTDLGPL ISPEAIGKVQ EHIADATDKG
     ARVVLGGGGD DMPGAFLRPT VLTGATQEMA VAREETFGPL AALFRFETEE EAIRLANDTI
     FGLASYVYAR DIGRVTRVQE GLDYGIVGVN TGLISTEVAP FGGVKQSGLG REGGHYGVEE
     FLEIKYVCTA V
//
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