ID A0A1Q5PXG8_9ACTO Unreviewed; 1190 AA.
AC A0A1Q5PXG8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN ORFNames=BSZ40_02115 {ECO:0000313|EMBL:OKL52303.1};
OS Buchananella hordeovulneris.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Buchananella.
OX NCBI_TaxID=52770 {ECO:0000313|EMBL:OKL52303.1, ECO:0000313|Proteomes:UP000185612};
RN [1] {ECO:0000313|Proteomes:UP000185612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20732 {ECO:0000313|Proteomes:UP000185612};
RA Meng X.;
RL Submitted (DEC-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 -!- 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:OKL52303.1}.
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DR EMBL; MQVS01000002; OKL52303.1; -; Genomic_DNA.
DR RefSeq; WP_073822863.1; NZ_MQVS01000002.1.
DR AlphaFoldDB; A0A1Q5PXG8; -.
DR STRING; 52770.BSZ40_02115; -.
DR InParanoid; A0A1Q5PXG8; -.
DR OrthoDB; 9812625at2; -.
DR Proteomes; UP000185612; 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:UP000185612}.
FT DOMAIN 134..424
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 526..944
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 453..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 724
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 758
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1190 AA; 129071 MW; 62769B9FEB570F81 CRC64;
MTTAAAARTE IDQAIMRAGQ TAQRWAAAAE QYSATRAAQL LGQALKDADG LDYTVQFVDK
VIRPEDLSVA ARNLAELAKR TPAFLPSWLK APARLGGVSG RLLPSVTIPA ARYVFRQLVG
DLVIDVTDEK LGPAIARLRE DGSRLNVNLL GEAVLGDKEA ARRLADTFKL LQRDDVDYVS
LKVSAVTGPH NPWAHAEVVA EAVERLAPLY DYAAAQPTPK FINLDMEEYR DLDMTIKVFT
KLLDRDNCLH LRAGIVLQAY LPDALPAMQR LQEWAAARRA RGGAPIKVRV VKGANLAMER
VAAEEKGWEL VTWESKTATD ANYLRVLEWA LTPQRMDAVH IGVAGHNLFT LAFAWELAGL
RGAREHLDVE MLAGMATPQA AAVRQDVGDL LLYVPVVRPA EYDVAIAYLV RRLEENAAPE
NFMASIFDIG HDTQAFAKEA ERFARAADMW QAEGERRVRP TRQQDRSSET ADQLTAAQQD
ADGRWRFANT PDSDPALPAN QRWARQILAR VPDSRLGEQT VAEAWIGAAD VADVLARATA
AGQQWAARPA RERAELLHRV GVELARRRGE LIEVAAAELG KGLDQADVEV SEAVDFAHYY
AERSRELEQL SGATFTPARV TLVTPPWNFP LAIPFGGVAA ALAAGCAVVL KPAPTARRCA
ALIAECLWAA GVPREVMQFV VGQDEEIGQP LVTDPRVERV VLTGASDTAE MFRNWRPDLP
LLAETSGKNA IIVTPSADLD LAVKDVVYSA FGHAGQKCSA ASLVILVGSA ARSKRFKNQL
VDAVQSLVVD WPTNPRAQVG PLSELPGDKL TRGLTVLEEG QNWVVRPRQL DDSGRLWSPG
VRAGVNAGSE FHLVEYFGPV LGVMRATTLA EAVELQNATQ YGLTAGLHSL DAKEINYWLD
HVQAGNVYVN RGITGAIVQR QPFGGWKRSA VGNGTKAGGP NYLLAFGTVT PAERTGGEEP
LTKPQLRELS RVALPLLEET VAVGVARDLA DLERACLTEF DVLHDPTGNA SERNILRYLP
ARATVRAEAD APLADIVRSL GAALAQGSFE LNEREDGTRI TRQAGGSKTG VPQLLLSTAT
PVPEALAEFA RRYGLDVRTE SAEEFRARTK RQLAAPEPGA PAQDVRVRLL GGSGARLLGD
LGGSIDVAVW ADPVTHCGRV EILPFVHEQA VSITNHRFGN PTPLTRQVLA
//