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
//