ID A0A0P9D6A2_9BACL Unreviewed; 516 AA.
AC A0A0P9D6A2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN ORFNames=AN477_04725 {ECO:0000313|EMBL:KPV44921.1};
OS Alicyclobacillus ferrooxydans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=471514 {ECO:0000313|EMBL:KPV44921.1, ECO:0000313|Proteomes:UP000050482};
RN [1] {ECO:0000313|EMBL:KPV44921.1, ECO:0000313|Proteomes:UP000050482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC-34 {ECO:0000313|EMBL:KPV44921.1,
RC ECO:0000313|Proteomes:UP000050482};
RA Hemp J.;
RT "Draft genome sequence of Alicyclobacillus ferrooxydans DSM 22381.";
RL Submitted (SEP-2015) 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 -!- 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:KPV44921.1}.
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DR EMBL; LJCO01000019; KPV44921.1; -; Genomic_DNA.
DR RefSeq; WP_054968023.1; NZ_LJCO01000019.1.
DR AlphaFoldDB; A0A0P9D6A2; -.
DR STRING; 471514.AN477_04725; -.
DR PATRIC; fig|471514.4.peg.3101; -.
DR OrthoDB; 9758906at2; -.
DR Proteomes; UP000050482; Unassembled WGS sequence.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-EC.
DR CDD; cd07124; ALDH_PutA-P5CDH-RocA; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR005932; RocA.
DR NCBIfam; TIGR01237; D1pyr5carbox2; 1.
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 SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KPV44921.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050482}.
FT DOMAIN 51..511
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 516 AA; 56103 MW; 8DA2D610D0CD275E CRC64;
MQTLMEYRNE PPLNFADPAT KAAMQAELAK VQGQLGQTYP LIIGGKRIQT TETSPSLNPS
NHNQVVGYVS QATKAHIDDA IAAAKEALET WRYTDPEIRA GYLFKAAAEI RRRKLEFAAW
QVYEVGKNWA EADGDVAEAI DFLEFYGRQM VRMAHPDPLV PFPAEMNHEV YAPLGIGVII
PPWNFPLAIL TGMTTSAIVA GNTVLLKPSP NSSVVGYKFM ELMKQIGLPD GVINFVPGAP
EEIGDYMTGH PDTAFVSFTG SKNVGLHIAE HASKRVSGQR GIKRVVAEMG GKDGILVDSE
ADLDAAALAI VQSAFGFQGQ KCSAGSRAII HKDVYDEVVN KVVEAAKGLQ VGTPDSNAAV
GPVIEKKQFD KIVGYIEIGK SEAKLVLGGT ADDSTGYYIN PTIFVDADPK SRIMQEEIFG
PVLAICKAES FEQAVDIFND TEYGLTGSVF SVNREHLRYA MERIECGNLY LNRKCTGSLV
GVHPFGGFKM SGTDAKAGSR DYLRHFVVSK IISERM
//
