ID A0A1M4SEL6_9ACTN Unreviewed; 1004 AA.
AC A0A1M4SEL6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN ORFNames=SAMN02745225_00245 {ECO:0000313|EMBL:SHE30694.1};
OS Ferrithrix thermotolerans DSM 19514.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Ferrithrix.
OX NCBI_TaxID=1121881 {ECO:0000313|EMBL:SHE30694.1, ECO:0000313|Proteomes:UP000184295};
RN [1] {ECO:0000313|Proteomes:UP000184295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19514 {ECO:0000313|Proteomes:UP000184295};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-
CC glutamate + NADH; Xref=Rhea:RHEA:30235, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58066; EC=1.2.1.88;
CC Evidence={ECO:0000256|ARBA:ARBA00001468};
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004786}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; FQUL01000002; SHE30694.1; -; Genomic_DNA.
DR RefSeq; WP_072787940.1; NZ_FQUL01000002.1.
DR AlphaFoldDB; A0A1M4SEL6; -.
DR STRING; 1121881.SAMN02745225_00245; -.
DR GeneID; 78385028; -.
DR OrthoDB; 9812625at2; -.
DR Proteomes; UP000184295; Unassembled WGS sequence.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0004657; F:proline dehydrogenase activity; IEA:InterPro.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:InterPro.
DR Gene3D; 3.20.20.220; -; 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; IPR025703; Bifunct_PutA.
DR InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR InterPro; IPR002872; Proline_DH_dom.
DR InterPro; IPR041514; PutA_N.
DR PANTHER; PTHR42862; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 1, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR42862:SF1; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 2, ISOFORM A-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF01619; Pro_dh; 1.
DR Pfam; PF18083; PutA_N; 1.
DR PIRSF; PIRSF000197; Bifunct_PutA; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF51730; FAD-linked oxidoreductase; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000184295}.
FT DOMAIN 14..126
FT /note="Proline utilization A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18083"
FT DOMAIN 139..443
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 532..984
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 764
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 798
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1004 AA; 110137 MW; 9FA07D98A3644EAF CRC64;
MSSVTKGADA PLQREIERFG AQVFKAAGSK TGIKELPLLA RQMMSFAMED PVFRSQLFRL
VDVFPTLRTD EEILSHMKEY FEGAQDGGRF AKIAAVGTRY ATSSKLSRGI TLSLTRKNLE
GVAQHFIAGT SPKEISKVLT RYRVEGILGT VDVLGEKTLT EPEAAAYATR VEELAAELEK
AASGWESTKL DFDTKGEFPK SSISVKSSAL SAHYHPLSAS VGIREVVNRF ETVLKSFGGD
SLIVFLDMED YETKPLTWEV FSTLVRDPRF MDYHLGLVVQ VYLRESLIDL NRFVSLSQER
VKMGGTPLWV RVVKGAYFDS ELVKAEAEGY QTPTFVHKVD SDYNFERAVD LLLGSIEYIR
PTFGSHNVRS ISYLHAKASE LNVPSSDYEV QMLYGMADDL AKAVAGLGKR VRMYIPMGEL
IPGMSYLVRR LLENTANEGF LRQGFASRGS YKALLKAPKP TSDYYRPSSS EHQLALDQPY
QHLGTLEFHR PHVSAEFGRA LQAISSRSKP YFPLTVPYVG GREIDRGAKE VSINPAHPGD
VVSEVINATS ELVDEAVSAA MAALSDWSRT PIERRAGYLM EAARWMHDRR KEIAALEVLE
AGKPWKEADA DVVEAIDFCN YYAHEMVRLG KGVGLLSPKG EHNDMFYRPK GVAAVIGPWN
FPLAIPTGMT VAALVAGNTV VLKPAEQTPA TAKVLVDAFR AVGLPDGVLN FLPGPGEEVG
AHLVRHKDVA VVAFTGSRSV GLEIIETASK WQKGQVHIKK VIAELGGKDA IIVDSDADLD
QVVPGVIYSA FGFSGQKCSA CSRLIVLRSS AEQVISRVIG AMDTLLVGDP QRPETDMGPL
IDYASQQRLK YYSDMAQSQG EVATAKLAIP DEGYYVLPSV ALELPKESPV LTEEIFGPLL
AVEIAEDLEE AVWLANSTDY ALTAGLFSRS PQNIEFIKNE LLAGNIYINR HITGAVPGRH
PFGGFKMSGI GSKSGGPDYL FQFLDPYVIS ENTVRQGFTP DIVN
//
