ID C0WH68_9CORY Unreviewed; 493 AA.
AC C0WH68;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Succinate-semialdehyde dehydrogenase {ECO:0000313|EMBL:EEI14988.1};
GN ORFNames=HMPREF0276_0804 {ECO:0000313|EMBL:EEI14988.1};
OS Corynebacterium accolens ATCC 49725.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=525260 {ECO:0000313|EMBL:EEI14988.1, ECO:0000313|Proteomes:UP000003641};
RN [1] {ECO:0000313|EMBL:EEI14988.1, ECO:0000313|Proteomes:UP000003641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49725 {ECO:0000313|EMBL:EEI14988.1,
RC ECO:0000313|Proteomes:UP000003641};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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:EEI14988.1}.
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DR EMBL; ACGD01000009; EEI14988.1; -; Genomic_DNA.
DR AlphaFoldDB; C0WH68; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_1_11; -.
DR Proteomes; UP000003641; 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; IPR029510; Ald_DH_CS_GLU.
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; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345}.
FT DOMAIN 24..482
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 261
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 493 AA; 52607 MW; DFF255BD9590DE04 CRC64;
MVMSINIEEV IAKVPTQLLI GGEWRDSTSG ETFDVENPAT GEKLATLASA NREDATAALD
AACAVQDEWA RTTPRERAEI LRRAFELVQE RAEDFAALMT LEMGKPIAES KGEVTYGGEF
LRWFSEEAVR DYGRTATVPE GTLRMITRRK PVGPCLLITP WNFPLAMATR KVAPAVAAGC
TMVLKPAKLT PLTAQYFAQT MLDAGLPKGV LNVVSGKSAS AISEPLLADA RLRKLSFTGS
TPVGRTLLKG AADNVLRTSM ELGGNAPFIV FEDADIDQAV KGAMGAKMRN IGEACTAANR
FLVHESVAEE FSEKLVAEFK KLKLGNGMDE GVTCGPLIEP KALDSVSGLV DDAAEKGATI
LTGGKRAGGD GYFYEPTVIS NVSRETRVSQ EEIFGPVAPI ITFSAEEEAL EIANDTEYGL
ASYVFTEDSD RLWRVADGLE FGLMGFNAGV ISNAAAPFGG VKQSGLGCEG GAEGIAEYTT
VQYLGIRDPY ANA
//