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Database: UniProt
Entry: A0A0Q5MUX0_9MICO
LinkDB: A0A0Q5MUX0_9MICO
Original site: A0A0Q5MUX0_9MICO 
ID   A0A0Q5MUX0_9MICO        Unreviewed;      1166 AA.
AC   A0A0Q5MUX0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE            EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN   ORFNames=ASF89_03830 {ECO:0000313|EMBL:KQR66264.1};
OS   Frigoribacterium sp. Leaf172.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Frigoribacterium.
OX   NCBI_TaxID=1736285 {ECO:0000313|EMBL:KQR66264.1, ECO:0000313|Proteomes:UP000051720};
RN   [1] {ECO:0000313|EMBL:KQR66264.1, ECO:0000313|Proteomes:UP000051720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf172 {ECO:0000313|EMBL:KQR66264.1,
RC   ECO:0000313|Proteomes:UP000051720};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQR66264.1, ECO:0000313|Proteomes:UP000051720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf172 {ECO:0000313|EMBL:KQR66264.1,
RC   ECO:0000313|Proteomes:UP000051720};
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   -!- 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:KQR66264.1}.
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DR   EMBL; LMPB01000001; KQR66264.1; -; Genomic_DNA.
DR   RefSeq; WP_055812165.1; NZ_LMPB01000001.1.
DR   AlphaFoldDB; A0A0Q5MUX0; -.
DR   STRING; 1736285.ASF89_03830; -.
DR   OrthoDB; 9812625at2; -.
DR   Proteomes; UP000051720; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051720}.
FT   DOMAIN          141..431
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
FT   DOMAIN          522..939
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   1166 AA;  123502 MW;  25D8D5C54AAC4F28 CRC64;
     MTTFDETAGP STAEQLLPVG IGDDAVALAR RWAHEASSAP STGSAHLLAQ VLKDESGLAF
     TIGFVDRVVR PEDLGVAARN LSTLAKQAPA FLPWHLRSAV RLGGVMAPVL PGVVVPIARR
     VLRGMVGHLI ADARPAELGA AIASIRRDRT RLNLNLLGEA VLGDAEAEHR LAGTRALLAR
     DDVDYVSIKV SSIVSQLSMW AFDETVERVI EKLTPLYELA ARSPEPKFIN LDMEEYRDLD
     LTIAVFTRLL GQPQLHGLEA GIVLQTYLPD ALGALQGLTD WATARVDAGG APIKVRVVKG
     ANLAMETVDA TVHEWPLATY GTKQDSDTNY KRVLTWALTP ERTRAVRIGV AGHNLFDIAF
     AHLLAEARGV SDRIEFEMLL GMAEGQAELV KNDVGGLLLY TPVVHPREFD VAISYLIRRL
     EENASSENFM SAVFELASNE TMFEREKGRF LASLAAVDGD TPAPHRVQSR LDPAQALAAR
     EPGSGFENEP DTDPALAANR AWGRDIAARS AHSTLGVDLI ESARVTDEAT LDTLLDRAVT
     ASAAWAARGG AGRAAVLRDA AAMLSARRAD LMEVAASETG KTVAEGDVEV SEAIDFANWY
     AHLAEELDSV DGARFVPERL TLVTPPWNFP IAIPAGSTLA ALAAGSSVVI KPAGQARRCG
     AVMVQALWDA GVPRDVLTLV DVDEGDLGRH LVSHPSVDRV VLTGAFETAQ LFTSWRNDLP
     LLAETSGKNS IIVTPSADLD LAASDVIKSA FGHAGQKCSA ASLVILVGSV ATSERFRRQL
     VDAASTMRVG LPSDPTTQMG PIVEPAHGKL ERALTTLGAG ESWLVEPRRL DETGRLWSPG
     VRTGVAAGSE FHLTEYFGPV LGIMTAATLD EAIALQNATD YGLTAGLHTL DPAELSVWLD
     AVEAGNLYVN RGITGAIVRR QPFGGWKKSS VGAGAKAGGP NYLVHLGSWQ PAAVVGTREA
     RPGSAVLAAV EAATPLLGAS GAAAADDLRA AAATDEHFWS TEFGVARDVS ALGLERDLLR
     YRPLPVTVRI ADGADPVDAV RVLLAGLRSG APLTVSTSID LPSAFVAALG RPVPVVAHES
     DEAWHDRVRA GGLRTERVRL VTGAGDADRA SSALSSALGG DPSVAVFDSA VTPTGRLELL
     PFLREQAIAI TAHRFGNPDP WSESVI
//
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