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Database: UniProt
Entry: G5R5H4_SALSE
LinkDB: G5R5H4_SALSE
Original site: G5R5H4_SALSE 
ID   G5R5H4_SALSE            Unreviewed;       522 AA.
AC   G5R5H4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Methylmalonate-semialdehyde dehydrogenase {ECO:0000313|EMBL:EHC82641.1};
GN   ORFNames=LTSESEN_4870 {ECO:0000313|EMBL:EHC82641.1};
OS   Salmonella enterica subsp. enterica serovar Senftenberg str. A4-543.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=913082 {ECO:0000313|EMBL:EHC82641.1, ECO:0000313|Proteomes:UP000005065};
RN   [1] {ECO:0000313|EMBL:EHC82641.1, ECO:0000313|Proteomes:UP000005065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A4-543 {ECO:0000313|EMBL:EHC82641.1,
RC   ECO:0000313|Proteomes:UP000005065};
RX   PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA   den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA   Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA   Furtado M.R., Wiedmann M.;
RT   "Genome sequencing reveals diversification of virulence factor content and
RT   possible host adaptation in distinct subpopulations of Salmonella
RT   enterica.";
RL   BMC Genomics 12:425-425(2011).
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:EHC82641.1}.
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DR   EMBL; AFCU01001573; EHC82641.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5R5H4; -.
DR   PATRIC; fig|913082.3.peg.3781; -.
DR   BioCyc; SENT913082:G120J-683-MONOMER; -.
DR   Proteomes; UP000005065; Unassembled WGS sequence.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd07113; ALDH_PADH_NahF; 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   PANTHER; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345}.
FT   DOMAIN          59..518
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        295
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   522 AA;  56694 MW;  8C4CDECFD4F3D061 CRC64;
     MTFFGTIFSS EKVCWDGKTY IPDLQALLMS DVTLLAEVTT FLRQRHGQFI AGERQAGNGT
     NFSVTNPATG KIIADVVSAT PAQAEEAMQS ARRAFDVWRK MPTLQRGALL LKLADTLAAH
     REELAQLESV CSGKTIMLSR GLELDQSVAF LRYFAGWAGK ITGETLNVSL PSMGEERYTA
     FTQRQPIGVV VGIVPWNFSI MIAIWKLAAA LVCGCTIVIK PSEYTPLTLL RVAELAKEAG
     FPDGVINVVN GAGGEIAQQL IAHPDCAKVS FTGSVATGEK VRRSATSSGK RVTLELGGKN
     AALFLNDLTA QAMVNGILEA GYLNQGQICA AAERFYLPQE KLDTVMTLLR QRLSEIVPGS
     PLDEKTVMGP LANQVQLEKV LHLIQRAREE GDTIVYGGET LPGEGYFLQP TAVKVRSKNS
     TLMHEETFGP VCSFIGYQNE KEALSHINAS PFGLAASVWS ENMSKALRYA EDIDAGMVWV
     NMHTFLDPAV PFGGMKGSGI GREFGSAFID DYTELKSVMV RY
//
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