ID V9XGX2_9NOCA Unreviewed; 1103 AA.
AC V9XGX2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN ORFNames=Y013_11400 {ECO:0000313|EMBL:AHD21230.1};
OS Rhodococcus pyridinivorans SB3094.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD21230.1, ECO:0000313|Proteomes:UP000018781};
RN [1] {ECO:0000313|EMBL:AHD21230.1, ECO:0000313|Proteomes:UP000018781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3094 {ECO:0000313|EMBL:AHD21230.1,
RC ECO:0000313|Proteomes:UP000018781};
RX PubMed=24874690;
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA Nielsen P.H., Nielsen J.L.;
RT "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL Genome Announc. 2:e00525-14(2014).
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; CP006996; AHD21230.1; -; Genomic_DNA.
DR RefSeq; WP_024102027.1; NC_023150.1.
DR AlphaFoldDB; V9XGX2; -.
DR GeneID; 29938968; -.
DR KEGG; rpy:Y013_11400; -.
DR PATRIC; fig|1435356.3.peg.2287; -.
DR eggNOG; COG0506; Bacteria.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005682_2_0_11; -.
DR Proteomes; UP000018781; Chromosome.
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 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 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}.
FT DOMAIN 122..413
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 501..916
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 437..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..467
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 701
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 735
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1103 AA; 121138 MW; 01B67EF005AC77BA CRC64;
MRIVEDAVAL ARRWVEESSE VAPDRAARHL ADVLKDPHGL EFTVRFVDEV IRPEDPATAA
HALAELSRNI PDFLPVHLRA AVRAGGTIGP RFPHLVVPAA RRALRAMVGH LVVDTDEAAL
GRAIARLRRP GIRLNLNLLG EAVLGDDEAR RRFEGTLALL ARDDVDYVSL KVSAAVAPHS
PWAFDETVAD IVERLAPLYR LAATSPTPKF VNLDMEEYHD LDVTVAAFTT LLDRPEFLHL
EAGIVLQAYL PDALTAMIEL QRWAASRRAR GGAAIKIRVV KGANLPMERV DASLHGWPLA
TWSTKQETDT NYKRLLHYAF TPERIENVRI GVAGHNLFDI AYAWELAGRR QVRNGIDFEM
LLGMAQSQAE VIRRHVGSLL LYTPVVRPDE FDVAISYLVR RLDEGSGQEN FMSAVFDLAD
DPALFEREEQ RFRASVAALD EDAPSPNRTQ NRQEPPIPAP PVFTNTPDTD PSLPQNREWG
RRILERVPSS KLGIDTVRAH ALSSEEQLER VLVDATAAGR AWGARSGAER ARILEQVADV
LEARRADLLE VMAAEGGKTL DQSDPEVSEA IDFARYYAER ARALDEIDGA RFVPSTLTVV
TPPWNFPVAI PAGSTLGALA SGSAVVLKPA TLTARCGSVL AEAMWDAGVP RDVLHLVHAD
ERSLGTKLVS DPRVDRVVLT GAYETAELFR SLRPGMRLLA ETSGKNAIVV TPSADPDLTV
RDVVQSAFGH AGQKCSASSL VILVGSVATS RRFRDQLVDA VRSLPVGPAH DPRTRMGPLI
EPARGKLLTA LTELEDGESW LVEPRRLDEE GRLWTPGVRT GVRRGSRTHL VEFFGPVLGV
MTAADLDEAI AIQNEVDYGL TAGLHSLDSD EIARWLDRVQ AGNVYVNRGI TGAIVRRQPF
GGWKKSSVGA GFKAGGPNYL FGFGSWEPCI WDEDTLRRAF EDDEQVWTSE FAVAHDVTGL
SAERNLFRYR PVRTHVRLGE AGRPDELVRV LGAAARAGAP VEISSAFALD LVRCSNTARF
GGRVRVESDV EWEERIVDTT PARVRLIGAA PPAEWNTRCD IAVFDHPVTG SGRIEMLPFL
AEQSVTITAH RFGTPHRLTD EII
//
