ID A0A0F4JPK8_9ACTN Unreviewed; 543 AA.
AC A0A0F4JPK8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=VR44_08220 {ECO:0000313|EMBL:KJY36307.1};
OS Streptomyces katrae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68223 {ECO:0000313|EMBL:KJY36307.1, ECO:0000313|Proteomes:UP000033551};
RN [1] {ECO:0000313|EMBL:KJY36307.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL ISP-5550 {ECO:0000313|EMBL:KJY36307.1};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-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}.
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:KJY36307.1}.
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DR EMBL; JZWV01000167; KJY36307.1; -; Genomic_DNA.
DR RefSeq; WP_045946730.1; NZ_JZWV01000167.1.
DR AlphaFoldDB; A0A0F4JPK8; -.
DR STRING; 68223.GCA_002028425_05013; -.
DR PATRIC; fig|68223.7.peg.4396; -.
DR eggNOG; COG1012; Bacteria.
DR OrthoDB; 6882680at2; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000033551; 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; 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Proline metabolism {ECO:0000256|ARBA:ARBA00023062}.
FT DOMAIN 55..526
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 543 AA; 58734 MW; 006CE7F7F10312E5 CRC64;
MDAVTQVPAP VNEPVHSYAP GSAERARLEI QLKQLSENPI DLPMTINGVK RMGGGERFDV
VQPHDHKSVI GTYANATQAD AQEAVDAALA AAPAWRAMSF DDRAAIILRA AELLAGPWRE
KLAASTMLGQ SKTAQQAEID TPCELVDFWR FNVHFARQIL AEQPAANSAG VWNRSDHRPL
EGFVYAITPF NFTAIAGNLP TAPALMGNVV VWKPSPTQTH SAVLLMELLE AAGLPKGVIN
LVTGDGIAVS EVALNHPELA GIHFTGSTKT FQYLWKTVGN NIEKYRSYPR LVGETGGKDF
VVAHPSADRA ILKTALTRGS FEFQGQKCSA SSRAYVPASI WNDGFKEQFA AEVDGITMGD
VRDLSNFIGA VIDERSFAKN KAAIDRAKAD PTCTIVAGGT YDDSEGYFVR PTVIECTDPE
NEVFTTEYFG PILAVHVYED DKYDEMLAQM ENVSAYALTG SVIAQDRYAA ADTMEKLRFA
AGNFYINDKS TGAVVGQQPF GGGRASGTND KAGAASNLLR WTSTRSIKET LVPPTEYGYP
HMG
//
