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Database: UniProt
Entry: Q1YN26_AURMS
LinkDB: Q1YN26_AURMS
Original site: Q1YN26_AURMS 
ID   Q1YN26_AURMS            Unreviewed;       495 AA.
AC   Q1YN26;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   SubName: Full=Succinate semialdehyde dehydrogenase {ECO:0000313|EMBL:EAS51205.1};
GN   ORFNames=SI859A1_02019 {ECO:0000313|EMBL:EAS51205.1};
OS   Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / SI85-9A1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Aurantimonadaceae; Aurantimonas.
OX   NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS51205.1, ECO:0000313|Proteomes:UP000000321};
RN   [1] {ECO:0000313|EMBL:EAS51205.1, ECO:0000313|Proteomes:UP000000321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS51205.1,
RC   ECO:0000313|Proteomes:UP000000321};
RX   PubMed=18344346; DOI=10.1128/AEM.01656-07;
RA   Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., Bernier-Latmani R.,
RA   McCarthy J.K., Torpey J.W., Clement B.G., Gaasterland T., Tebo B.M.;
RT   "Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium
RT   Aurantimonas sp. strain SI85-9A1.";
RL   Appl. Environ. Microbiol. 74:2646-2658(2008).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986}.
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:EAS51205.1}.
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DR   EMBL; AAPJ01000001; EAS51205.1; -; Genomic_DNA.
DR   RefSeq; WP_009209847.1; NZ_CH672387.1.
DR   AlphaFoldDB; Q1YN26; -.
DR   HOGENOM; CLU_005391_1_0_5; -.
DR   OrthoDB; 9812625at2; -.
DR   BioCyc; AURANTIMONAS:SI859A1_02019-MONOMER; -.
DR   Proteomes; UP000000321; 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; 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; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000321}.
FT   DOMAIN          33..490
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   495 AA;  52343 MW;  75A0A7A9031F3801 CRC64;
     MSAAIRHLDT LHPLAALDDA TLFVQAAFLA GRWITSDATV AVTDPATGET LGFIPALTAA
     DTGRAIDAAE AALPAWRALL PQERARILKR WHDLILASRE DLALLMTLEQ GKPLAESRGE
     IDYAASFVDY YAEEARRVAV EGLTSHLPNA QMTLCRVPLG VVGLVTPWNF PAAMLTRKAA
     AALAAGCTTV AHPSSETPFS ALALAALAER AGMPAGVFNV VTGNAATIVG RLCEDRRVRA
     MSFTGSTEIG RLIAAQAAPT VKRLIMELGG HAPLMIFADS DLDRAVDIAM DAKFATSGQD
     CLAANRIYVE RSIYEPFLAA FKARIAALAV GPGLSASTEI GPLMHARAIA KVEAQVHDAV
     GRGARCLAGG GRDAAGPLFY RPTLLADVPE DALIMHEETF GPVAAVTPFD TEDEVLARAN
     DTEYGLVAYL VTRDAARIAR MTAALEYGMV AVNRVKITGT PIPFGGVKQS GMGREGARHG
     LEAFTDLKYV CQDIG
//
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