ID A0A1B7LXI0_9MICC Unreviewed; 1180 AA.
AC A0A1B7LXI0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN ORFNames=A6F49_14040 {ECO:0000313|EMBL:OAV59873.1};
OS Enteractinococcus helveticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae.
OX NCBI_TaxID=1837282 {ECO:0000313|EMBL:OAV59873.1, ECO:0000313|Proteomes:UP000078292};
RN [1] {ECO:0000313|EMBL:OAV59873.1, ECO:0000313|Proteomes:UP000078292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UASWS1574 {ECO:0000313|EMBL:OAV59873.1,
RC ECO:0000313|Proteomes:UP000078292};
RA Crovadore J., Chablais R., Lefort F.;
RT "First whole genome shotgun sequence of the bacterium Enteractinococcus sp.
RT strain UASWS1574.";
RL Submitted (APR-2016) 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 -!- 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:OAV59873.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LXEY01000021; OAV59873.1; -; Genomic_DNA.
DR RefSeq; WP_043058365.1; NZ_LXEY01000021.1.
DR AlphaFoldDB; A0A1B7LXI0; -.
DR STRING; 1837282.A6F49_14040; -.
DR OrthoDB; 9812625at2; -.
DR Proteomes; UP000078292; 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; 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.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 135..428
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 518..947
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 724
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 758
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1180 AA; 128815 MW; 2B1E99CB0269E1D7 CRC64;
MQTPAHATSE ITPWQLGDQA IEQVRTWLAQ AANIKPDASA QQLAGVLKDP NGLDFTVGFV
DRVVRPEDHH AAASALAHIA YDVPAFLPWY LQSAVRTGGK LAEVAPGVVV PAAQAALRAM
VGHLIIDSRD KQLGKAIKRL RTDGIDLNIN LLGEAILGQG EADNRVAATL ALIHRHDVDY
VSIKVSATVA PHNHWAHDEA VENIVQQLRP LYRAAMTSDP VTFINLDMEE YKDLDLTIDV
YRRLISEPEF KHFRTGIVLQ AYLPDAYQAM VGLQEFAAQR VAAGGAPIKV RVVKGANLPM
EKVKAAMHHW PQTVWPTKQD TDTNYKRILN HALTPERLTN VEIGVAGQNL FDIALAYLLM
QHRNIPIDGP VDFEMLLGMA TTQAQAIRAD VGRLLLYTPV VHPDEFDVAI SYLVRRLEEG
ASHENFMSAV FDLDNPVIFD RETQRFQASL AQLEAEADLV PQPRRQQNRA TEHFEKASPV
EFHNAADTDP DLPQNRDWAG AILGRMADSE LGDDLVSSHQ VTNQKQLDEV IDSAIAAGET
WRKLPLETRS RVLIRIGDHL AANRGRLIEV MGSETGKTID QADPEVSEGI DFARYYGQQC
LELDNIAGAK PHPVGLTVVT PPWNFPMAIP TGSMTSALAT GSPVIIKPAP QAQRTAAVIV
QAIWDAFDEF ELPHEILTFV IAEENSLGSN LVTDQRVERV ILTGGYETAK LFTDLRPDMP
LFGETSGKNA IIVTPSADLD LAVADVVNSA FGHAGQKCSA ASLVILVGQT ARSKRFHRQL
LDAVNSLVVD YPTNPEAQMG PVIEPPGEKL TRGLTTLEHG QRWHLRPRLL DDSGQLYSPG
VRSGVQPGSE YHMTEYFGPV LGVMSAETLD EAIEYVNAVP FGLTSGIHSL DPDEIALWTE
HVAAGNLYIN RGITGAIVQR QPFGGWKRSA IGPGAKAGGP NYLLSLTDWT DAPDTVSAAQ
DDIADQLEAT IGSVLDSADL KWLTQAVAHD ATAVETYTGQ RDISNLHVEI NVLRYRPVPV
TMRVTDTGST TLAQAIRVGY AGIRAQRAVA SGQGTGALPM NTVSLPADTP EAITKVFNAT
NVRVVFDDTT SWLERARRLA QADPTKGSQR IRLIGDDETD ETIKATAQTP EIAVYRQPVT
SAGRLEMLPF LREQAVTMTA HRFGTINDLP QRALGDIQFG
//
