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Database: UniProt
Entry: G9ZTU2_9LACO
LinkDB: G9ZTU2_9LACO
Original site: G9ZTU2_9LACO 
ID   G9ZTU2_9LACO            Unreviewed;       475 AA.
AC   G9ZTU2;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Putative succinate-semialdehyde dehydrogenase {ECO:0000313|EMBL:EHL95205.1};
GN   ORFNames=HMPREF9103_03177 {ECO:0000313|EMBL:EHL95205.1};
OS   Lentilactobacillus parafarraginis F0439.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lentilactobacillus.
OX   NCBI_TaxID=797515 {ECO:0000313|EMBL:EHL95205.1, ECO:0000313|Proteomes:UP000004625};
RN   [1] {ECO:0000313|EMBL:EHL95205.1, ECO:0000313|Proteomes:UP000004625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0439 {ECO:0000313|EMBL:EHL95205.1,
RC   ECO:0000313|Proteomes:UP000004625};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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:EHL95205.1}.
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DR   EMBL; AGEY01000211; EHL95205.1; -; Genomic_DNA.
DR   RefSeq; WP_008215478.1; NZ_JH415063.1.
DR   AlphaFoldDB; G9ZTU2; -.
DR   STRING; 797515.HMPREF9103_03177; -.
DR   PATRIC; fig|797515.3.peg.2886; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_9; -.
DR   Proteomes; UP000004625; Unassembled WGS sequence.
DR   GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro.
DR   CDD; cd07100; ALDH_SSADH1_GabD1; 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   InterPro; IPR044148; ALDH_GabD1-like.
DR   InterPro; IPR047110; GABD/Sad-like.
DR   PANTHER; PTHR43217; SUCCINATE SEMIALDEHYDE DEHYDROGENASE [NAD(P)+] SAD; 1.
DR   PANTHER; PTHR43217:SF2; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE [NADP(+)]; 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          3..442
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        229
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   475 AA;  51742 MW;  49BCC4F4136CEDA2 CRC64;
     MAYRTVNPYN NEVVKEYPFA TDDQLQDALA TGHDLYETMK KQPIADRAKI LHNVAAKLRE
     HEDELARACT IDMGKLIGES RGEVELVAII ADWFADHGEE ILKPEKIDTI ATGEAEIQHH
     ATGVIMMVEP WNFPYYQIMR VFAPNFIVGN PMILKHAANT PTSAQMFADV VAEAGAPKGS
     LTNLFLSYDQ VTEAIDDPRV QGVALTGSER GGTSVAGAAG KALKKNTMEL GGMDPFVVLG
     DANMDDVADI AWRARIYNTG QVCTSSKRFI VMDNVYDQFV DVLKDKFSQL KPGDPLDPNT
     TLAPMNTKKA KEKLQGQLDD AIAHGAKVVY GNEPIDLPGQ FFRPTILTDI SKDNPAYKTE
     LFGPIACVYK VHSEEEAIEV ANDNPYGLGG IVFAGDADHG AEVASQIETG MVFVNNFMST
     LPELPFGGVK LSGYGREMSH IGEFAFVNEQ LIVKADKPNL KNPAGGLVAF GPDDQ
//
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