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Database: UniProt
Entry: A0A1Q5PXG8_9ACTO
LinkDB: A0A1Q5PXG8_9ACTO
Original site: A0A1Q5PXG8_9ACTO 
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
//
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