ID Q98AY0_RHILO Unreviewed; 497 AA.
AC Q98AY0;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE SubName: Full=Succinic semialdehyde dehydrogenase {ECO:0000313|EMBL:BAB52192.1};
GN OrderedLocusNames=mll5809 {ECO:0000313|EMBL:BAB52192.1};
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB52192.1, ECO:0000313|Proteomes:UP000000552};
RN [1] {ECO:0000313|EMBL:BAB52192.1, ECO:0000313|Proteomes:UP000000552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC {ECO:0000313|Proteomes:UP000000552};
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR EMBL; BA000012; BAB52192.1; -; Genomic_DNA.
DR RefSeq; WP_010913527.1; NC_002678.2.
DR AlphaFoldDB; Q98AY0; -.
DR KEGG; mlo:mll5809; -.
DR PATRIC; fig|266835.9.peg.4621; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_5_1_5; -.
DR Proteomes; UP000000552; Chromosome.
DR GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro.
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; 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; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345}.
FT DOMAIN 36..491
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 269
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 497 AA; 54325 MW; 139209E5ED061105 CRC64;
MKGDDGLTVT QSLTRRLKNP ELFDDLAGVP GRKAEQSTRR FSVFNPSTGE LLAELPDMDV
RDVSKAIDKA EAAQEHWAAL TARERSDILW EWHQLILDHS EDLAAILTAE MGKPLAEAKS
EIAHAAAYLQ WYAEEANRIY GETISPPSND RRMLVIKQPI GVVGAITPWN FPASMVARKI
SPALAAGCAI VLKPAEQTPL VAGAMFTLAR MAGFPDGVLN LIYASEGDAV GRELCSNPKV
RKISFTGSTE VGRLLMRECS DQIKRTSFEL GGNAPFIVFD DADVDAAVDG ALQAKFRNAG
QTCVSANRLY VQSSVYNEFC DKFTKRVSAL RVGDGFEPEV AIGPLIDKCA LAKIEDHIRD
AVRQGGKIRC GGNRIGESGT FFEPTVITDV ERTMRVAQEE TFGPLAPIIR FNDPDQVVRE
ANDTIYGLAA YFYASNLKRV WRVAEALEYG MVGINTGRMS SEAAPFGGMK QSGIGREGSR
HGLEDYLEMK YLCMGGL
//
