ID A0A0Q3WR75_9BACI Unreviewed; 543 AA.
AC A0A0Q3WR75;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00032259};
GN ORFNames=AN964_23075 {ECO:0000313|EMBL:KQL50543.1};
OS Heyndrickxia shackletonii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX NCBI_TaxID=157838 {ECO:0000313|EMBL:KQL50543.1, ECO:0000313|Proteomes:UP000051888};
RN [1] {ECO:0000313|EMBL:KQL50543.1, ECO:0000313|Proteomes:UP000051888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 18435 {ECO:0000313|EMBL:KQL50543.1,
RC ECO:0000313|Proteomes:UP000051888};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
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 -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, 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:KQL50543.1}.
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DR EMBL; LJJC01000015; KQL50543.1; -; Genomic_DNA.
DR RefSeq; WP_055742154.1; NZ_LJJC01000015.1.
DR AlphaFoldDB; A0A0Q3WR75; -.
DR STRING; 157838.AN964_23075; -.
DR PATRIC; fig|157838.3.peg.5068; -.
DR OrthoDB; 9762913at2; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000051888; Unassembled WGS sequence.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
DR CDD; cd07123; ALDH_F4-17_P5CDH; 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; IPR005931; P5CDH/ALDH4A1.
DR NCBIfam; TIGR01236; D1pyr5carbox1; 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.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Proline metabolism {ECO:0000256|ARBA:ARBA00023062};
KW Reference proteome {ECO:0000313|Proteomes:UP000051888}.
FT DOMAIN 58..512
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 293
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 543 AA; 59823 MW; 45441751D605B044 CRC64;
MSNGIFKIPT PKNEPGNTYA PGTKERETLK AELKRQSDIV VDIPVIINGE NIKTDTVKQV
VMPHDHKHVL ANYSQAGEKE LRESIEAAMA AKEAWANMPW EHRASIFLKA ADLISGPYRD
LINASTMLGQ SKTAYQSEID AAQELVDFLR YDVDCANQIY QIQPSSAKNI WNRTDYRPLD
GFVLAISPFN FTSIGANLPV APAIMGNVVV WKPATTSLLS NYYFMRVLEE AGLPKGVINF
VPSRGSQVSE VVLTDPRMSG FHFTGSTSTF QTIWKTVGEN IANYQSYPRL IGETGGKDFV
FVHETAQVDK VVANLVRGAF EYQGQKCSAA SRAYIPASLW EEVKSGLVEE TAKLKVGDIQ
DFRNFMGAVI DKAAFDSITS YIDFAAASEE AEIIAGGTYD DSVGYFVQPT IIVTTNPNFK
TMVEEIFGPV LTIYVYENDK LEETLEAVDT ASIYALTGAI FAQDREAIIH LERRLSGAAG
NFYINDKPTG AMIDQQPFGG SRGSGTNDKA GSVFNMVRWT SPRVIKENFA PTAEVAYPFM
DAE
//
