ID K7S318_ACIA4 Unreviewed; 1200 AA.
AC K7S318;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN OrderedLocusNames=PACID_11380 {ECO:0000313|EMBL:AFV88962.1};
OS Acidipropionibacterium acidipropionici (strain ATCC 4875 / DSM 20272 / JCM
OS 6432 / NBRC 12425 / NCIMB 8070 / 4) (Propionibacterium acidipropionici).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Acidipropionibacterium.
OX NCBI_TaxID=1171373 {ECO:0000313|EMBL:AFV88962.1, ECO:0000313|Proteomes:UP000000214};
RN [1] {ECO:0000313|EMBL:AFV88962.1, ECO:0000313|Proteomes:UP000000214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4875 / DSM 20272 / JCM 6432 / NBRC 12425 / NCIMB 8070
RC {ECO:0000313|Proteomes:UP000000214};
RX PubMed=23083487; DOI=10.1186/1471-2164-13-562;
RA Parizzi L.P., Grassi M.C., Llerena L.A., Carazzolle M.F., Queiroz V.L.,
RA Lunardi I., Zeidler A.F., Teixeira P.J., Mieczkowski P., Rincones J.,
RA Pereira G.A.;
RT "The genome sequence of Propionibacterium acidipropionici provides insights
RT into its biotechnological and industrial potential.";
RL BMC Genomics 13:562-562(2012).
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; CP003493; AFV88962.1; -; Genomic_DNA.
DR AlphaFoldDB; K7S318; -.
DR STRING; 1171373.PACID_11380; -.
DR KEGG; pbo:PACID_11380; -.
DR PATRIC; fig|1171373.8.peg.1135; -.
DR eggNOG; COG0506; Bacteria.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005682_2_0_11; -.
DR Proteomes; UP000000214; Chromosome.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0004657; F:proline dehydrogenase activity; IEA:UniProtKB-EC.
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 190..480
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 562..982
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 511..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 766
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 800
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1200 AA; 128399 MW; 3149DC5717A9607A CRC64;
MMMRLILSAP EGGCPAHPNG SASVVEQFGV LATPAGDGRY RLGMGSEGDE QRWTSPDPAP
ADLADEAVAQ VHRWLERTPG QGRTPRFDRG RAAARLLSQV LSEPSGLPFT VGFIDQVMRP
EDPVTAARSL TRLSRTDCSF LPAPLRLGVR IAGRLAPVAP GLVVRASRMV LRQLVGHLVV
DSRPVMLGRS LRRLRGDGVR LNLNLLGEAV LGDREAAERL SGIERLLARP DVDYVSVKIS
SVVNQLDLWA HDQTVARVAD RLSPLFQLAA DSADQKFINL DMEEYHDLDL TIDVFTALLD
RPEFLHLEAG IVIQAYLPDA LAAVQRLTRW AERRAAAGGA GIKIRLVKGA NLPMEKVDAE
RHGWAQAPWG SKVATDANYK RVLDWALTPD RTRSVRYGIA GHNLFDIALA RGLAAGRGVS
DRVEFEMLAG MAPDQVERIK QDVGGVLLYT PVVHPDHFDV AISYLVRRLE ENAAEENFMS
AVFDIGDDET LFAREEERFR AAVAAATRVV PGPNRHQTPD RVPEGPGFTW STDSDPALPV
NRAWARDVAA AMPGCRLGTT TLNTHRVETA DQVDAAVATA LGAAPGWAEA GASARADVLH
RVAAELARRR GDLLAVAGHE TGKVFEQGDV EVSEAIDFAD WYADQAGLLE QVDGARYVPA
RVSVVAPPWN FPLAITTGST LAPLATGSAV ILKPAPQARQ CAAVIAECMW AAGVPREVLQ
LVDAGEGEAG RRLISHPDVD RVILTGAHDT AKLFRSWRPD LPLLAETSGK NAIIVTENGD
YDLAAADIIA SAFGHAGQKC SAASLVILVG QAYRSKRLRT QIIDAAASLR VGGPEDLTTQ
LGPVIEPAAG KLLDGLTRLD PGQNWALEPR RLDESGRFWS PGIRAGVGAG DRYHLTEYFG
PVTGIMYAPD LATAVAYQNG TEYGLTAGLH SLDPEEISWW CDHVNAGNLY VNRGITGAIV
GRQPFGGWKK SAVGPGAKAG GPNYLAVLGG WEPIAAVAPT PEARICDRVD RFIAHVATGL
AQGSERLRDA AARDARAWEE EFGISRDIGG LELERNEFRY RPAPTLIRIC PDADPVDAAR
VCAAGILAAG ELLSVSVDPV AGHLLVGALT SLGIACDVVA QADWLVSMRA PGAPRRVRLV
GGDSSQLAGA VAGDPDLAVW AWPVTSAPRV ELLAFLREQS ISLTGHRFGS PSAAIGSVQL
//
