ID A0A0J6CT19_9BACI Unreviewed; 515 AA.
AC A0A0J6CT19;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=1-pyrroline-5-carboxylate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00733};
DE Short=P5C dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00733};
DE EC=1.2.1.88 {ECO:0000256|HAMAP-Rule:MF_00733};
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00733};
GN Name=rocA {ECO:0000256|HAMAP-Rule:MF_00733};
GN ORFNames=AB986_09785 {ECO:0000313|EMBL:KMM39461.1};
OS Alkalihalobacillus macyae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=157733 {ECO:0000313|EMBL:KMM39461.1, ECO:0000313|Proteomes:UP000035996};
RN [1] {ECO:0000313|EMBL:KMM39461.1, ECO:0000313|Proteomes:UP000035996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16346 {ECO:0000313|EMBL:KMM39461.1,
RC ECO:0000313|Proteomes:UP000035996};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Zheng C., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RL Submitted (JUN-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, ECO:0000256|HAMAP-
CC Rule:MF_00733};
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, ECO:0000256|HAMAP-Rule:MF_00733}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. RocA
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00733}.
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:KMM39461.1}.
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DR EMBL; LELK01000001; KMM39461.1; -; Genomic_DNA.
DR RefSeq; WP_048310632.1; NZ_LELK01000001.1.
DR AlphaFoldDB; A0A0J6CT19; -.
DR STRING; 157733.AB986_09785; -.
DR PATRIC; fig|157733.3.peg.4263; -.
DR OrthoDB; 9762913at2; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000035996; Unassembled WGS sequence.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
DR CDD; cd07124; ALDH_PutA-P5CDH-RocA; 1.
DR HAMAP; MF_00733; RocA; 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; IPR005932; RocA.
DR InterPro; IPR047597; RocA_bacillales.
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.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|HAMAP-Rule:MF_00733};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00733}; Reference proteome {ECO:0000313|Proteomes:UP000035996}.
FT DOMAIN 49..511
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 286
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00733,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 320
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00733"
SQ SEQUENCE 515 AA; 56447 MW; CD024D6D63FB0B7C CRC64;
MVVPYKHEPF TDFTVKENKK AFEEALKLVK EELGKDHDLL INGERVSTED KIVSINPANK
EQVVGRVSKA TKEHAERAIQ AADEAFEGWR KWSARSRAEL LFRAAAIVRR RKHEFSAYLV
YEAGKPWKEA DADTAEAIDF MEYYARQMIE LGEGKAIESR PGEQNRYVYT PSGVALVIPP
WNFAFAIMAG TAVAPLVTGN TVLLKPASAT PVVAAKFVEV LEEAGLPKGV LNFVPGSGAE
VGDYLVDHPK TSIITFTGSR EVGTRIYERA AKVQPGQQHL KRVIVEMGGK DTIVVDKDAD
LELAAQAIVV SAFGFSGQKC SAGSRAVILK EVYDQVRDRV VELTNELTLG ETTGPDVYMG
PVIDQASFDK IMSYIEIGKE EGRLVAGGEG DDSKGYFIKP TVFADLAPKS RMQQEEIFGP
VVCLTKADNF DEAIEIANNT EYGLTGAVIT NNRAHIEQAK MDFHVGNLYF NRNCTGAIVG
YHPFGGFKMS GTDSKAGGPD YLGLHMQAKT VSEMF
//
