ID Q13PI3_PARXL Unreviewed; 496 AA.
AC Q13PI3;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Succinate semialdehyde dehydrogenase {ECO:0000313|EMBL:ABE34006.1};
DE EC=1.2.1.16 {ECO:0000313|EMBL:ABE34006.1};
GN ORFNames=Bxe_B1976 {ECO:0000313|EMBL:ABE34006.1};
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE34006.1, ECO:0000313|Proteomes:UP000001817};
RN [1] {ECO:0000313|EMBL:ABE34006.1, ECO:0000313|Proteomes:UP000001817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400 {ECO:0000313|EMBL:ABE34006.1,
RC ECO:0000313|Proteomes:UP000001817};
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CP000271; ABE34006.1; -; Genomic_DNA.
DR AlphaFoldDB; Q13PI3; -.
DR STRING; 266265.Bxe_B1976; -.
DR KEGG; bxe:Bxe_B1976; -.
DR eggNOG; COG1012; Bacteria.
DR Proteomes; UP000001817; Chromosome 2.
DR GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
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}.
FT DOMAIN 27..485
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 263
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 496 AA; 53192 MW; CFA9E6B4F4C88BD6 CRC64;
MTNHPTAMPS LQEPSLFRQE CYIAGEWIES DPMARIDVVN PANGLKIGTV PRATLADVRT
CIDAAERALP AWSGKTGKER AAILRRWYEL MLQHQEDLAV IMTCEQGKPL AESRGEIVYA
ASFLEWFAEE AKRVYGDTIP TPASDRRIVV LKQPIGVCAA ITPWNFPAAM LTRKIGPALA
AGCTMVLKPA SQTPFSALAL CVLAERAGVP AGVLSCVTGK ASMIGDEFCR NPAVRKLSFT
GSTEIGKLLL QQCASTVKKT SMELGGNAPF IVFDDADLDA AVVGAIAAKF RNAGQTCVCV
NRFLVQDTVH DAFVEKLSTA IAALKVGDGL DAGTRIGPLI DSKAVEKARE HVDDAIARGA
TVVTGGSGHA LGGNYFEPTL LTGASKDMKI FREETFGPVA PVFRFRTEEE AIQLANDTEF
GLASYFYGRD IGRVWRVAEA LEYGMVGINE GLISTEVAPF GGVKESGLGR EGSKYGIEDY
LEVKYLCMGG LAARPV
//
