ID A0A0Q9D703_9CELL Unreviewed; 1162 AA.
AC A0A0Q9D703;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-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};
GN ORFNames=ASE27_03710 {ECO:0000313|EMBL:KRD47736.1};
OS Oerskovia sp. Root918.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Oerskovia.
OX NCBI_TaxID=1736607 {ECO:0000313|EMBL:KRD47736.1, ECO:0000313|Proteomes:UP000051694};
RN [1] {ECO:0000313|EMBL:KRD47736.1, ECO:0000313|Proteomes:UP000051694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root918 {ECO:0000313|EMBL:KRD47736.1,
RC ECO:0000313|Proteomes:UP000051694};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRD47736.1, ECO:0000313|Proteomes:UP000051694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root918 {ECO:0000313|EMBL:KRD47736.1,
RC ECO:0000313|Proteomes:UP000051694};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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|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:KRD47736.1}.
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DR EMBL; LMJG01000001; KRD47736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q9D703; -.
DR Proteomes; UP000051694; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051694}.
FT DOMAIN 129..422
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 519..973
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 432..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 750
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 784
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1162 AA; 122447 MW; 1835BAAC718017CC CRC64;
MADLTDDAAR LARSWIAAAE AASEGARERR TAERLGALVS DPAGLELAVR FVDNVARPQD
VQVAARELGL LGELAGGAKG FLGPVDTTLL RLGARMAPVL PTVVVPAARI RLRQLVGHLV
ADAGPGLGKH LARTRAEGYA LNVNLLGEAV LGEDEAQARL ARTIALVERP DVDYVSVKVS
SVASQLVTWD LEGSRDRVVE RLLPLFRAAR DHGVFLNLDM EEYRDLALTT EVFQAILGRE
EFRALEAGIV LQAYLPDALG ALDGLTAFAT ERVAAGGAPV KVRLVKGANL AMEKVEAELH
GWEQAPYPTK PDVDANYVRL VDHALRAPRT DAVRIGVASH NLFHVALAIL AARARGVSHA
LDIEMLQGMA PGEARAVRDE VSRDGGRVVL YTPVVAREDF DVAISYLVRR LEENAAEQNF
LHAMFAPATD PVSELDRARD RAGSDNSAGS AMDRQEAAYR ASVLLGTQYA DADVTPRRRV
RDAVGPRDAA TPDRTVGSGF RNASDTDPAV AANRAWAARV VGPDSGYVPA QSPEVTSTDE
VDDVVARAEK AAAAWAQVAP ADRARALRAV AVRLEDARTA LVTAMVHEPG KTVAEADPEV
SEAVDFASYY ARSAEALDQV PGATFTPDGV TLVTPPWNFP VAIPVGGIVA ALAAGSAVVA
KPAPATPRCL EVAVDAIHAG LADAVADAPA GSSLTPEAVR DVVQLSRVPD GDLGRHLVTH
EGVARVILTG AIETAQMFAS WRPGLDVLAE TSGKNAIVVT PSADLDLAAA DVVRSAFGHA
GQKCSAASLV ILVGSVGDQR TETGRRFSVQ LVDAVRSLAV GPATDVSTTM GPLTEVAEGK
LLRALTTLEP GEQWLVAPRR LDEDGRLWTP GLRSGVAPGS FFHLTEVFGP VLGVMTAATL
DEAIELQNAV SFGLTGGIHS LDDAEVDTWL DRVQVGNAYV NRVITGAIVQ RQSFGGWKRS
AVGPGAKAGG PNYVAELGMW SDAVVPGEGP AGGLPDGGPV PARETSPEAW LAWARADDAR
WWAHEFAVEH DPSGLHVESN LFRYRPIDVL TVRVGTGAAP VEVERVLSAA RTAGVPVVVS
RADGPSAVSD EDFAAAVARG EVTGRVRVVG AAPGLREAAA GRVGDVTVLD HPVLASGRRE
LLTVLREQAI SRTMHRFGHV TR
//
