ID A0A0W7WBB7_9MICO Unreviewed; 1185 AA.
AC A0A0W7WBB7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN ORFNames=AUL38_00850 {ECO:0000313|EMBL:KUF07853.1};
OS Leucobacter sp. G161.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=663704 {ECO:0000313|EMBL:KUF07853.1, ECO:0000313|Proteomes:UP000053012};
RN [1] {ECO:0000313|EMBL:KUF07853.1, ECO:0000313|Proteomes:UP000053012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G161 {ECO:0000313|EMBL:KUF07853.1,
RC ECO:0000313|Proteomes:UP000053012};
RA Ge S., Dong X.;
RT "High quality draft genome sequence of Leucobacter sp. G161, a distinct and
RT effective chromium reducer.";
RL Submitted (DEC-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 -!- 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:KUF07853.1}.
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DR EMBL; LOHP01000046; KUF07853.1; -; Genomic_DNA.
DR RefSeq; WP_059059440.1; NZ_LOHP01000046.1.
DR AlphaFoldDB; A0A0W7WBB7; -.
DR STRING; 663704.AUL38_00850; -.
DR OrthoDB; 9812625at2; -.
DR Proteomes; UP000053012; 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:UP000053012}.
FT DOMAIN 131..421
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 528..954
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 732
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 766
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1185 AA; 126163 MW; C88BAB1DC4C91866 CRC64;
MSQATPRPQD LAEESIALAR KWITEAASIP TDASAARLAG VLRDPNGLDF TVGFVDGVVR
PEDLSVAAKK LKELVPLTPG FLPGVMRGAI GMGGAFAKPL PGVVVPIARK VLRQMVSHLI
IDATDSKLGP AISKIQTEGV RLNMNLLGEA ILGQGEAERR LAGTHKLLAR PDVDYVSIKV
SSTVAPHNHW AFDEAIEHIE SQLIPLFERA AAASPQKFIN LDMEEYKDLD LTLEVFMRIL
DRPEFLNLEA GIVLQAYLPD ALGAMMRLQE WSAKRVARGG ASIKVRLVKG ANLPMELVDA
AVHGWPAATW GTKQDSDTSY KAVLDYSLTP EHVKNVRIGV AGHNLFDLAL AWLLAKGRGA
ESGLEVEMLL GMATGQAEAV RRDVGSLLLY VPVVHPDEFD VAISYLIRRL EEGASQENFM
SAVFEVHENK ELFDREKNRF LASLDDLAAI TADGDPANYS VPPSNRVQDR RAYDAAGAEA
RVEALVAKGR KGEFDNAPDS DPDLPGNHVW GREIADRMVS STLGDNLVAE ALVESAQDLD
EIVARGVAAA DGWQALGADE RARILYRAGE ALEARRGALL EVMGSECGKT LDQGDPEVSE
AIDFANYYAM LGQVIGQVDG ATYKQQKLTA VIPPWNFPVA IPAGGALSAL AAGSAVIIKP
ASNSARSGAV MIEALWEAGV PRDVLQFVQF ADRALGSKLV ADPRVDRLIL TGAYETAVNF
RELRQDLPIL AETSGKNAII VTPNADLDLA AKDVVQSAFG HAGQKCSAAS LVILVGSVAT
SKRFRGQLLD AARSLKIGTP ENLETQMGTI ITAPDGKLLR GLTTLSAGEK WLIEPKPLKS
DSPLAADKKG NNKLWNPGVR EGVKRGSEYH LTEYFGPILG IMTAETLDEA IDMVNEIDYG
LTSGLHSLDR DEMALWLDRI QAGNLYINRG ITGAIVRRQS FGGWKKSAIG AGTKAGGPSY
LYGLGAWEDA PVTAALTAPR PAAAPILTAA QQAGVSGAEL EWLRAALGTD ATAWNDEFGI
ARDASGVGVE RNLLRYKPVP VTVRAAADAP IHHTIRVVAA GIAAGSRPTV STPAALPEPI
SKAFKAAGVE IQFEDDAAWA ARLGRIAAQD GPNASARIRL VAGASRADGL AAITAATGGK
PDIAVYGGDI VSAGRVEMLP FMHEQAVSIT AHRFGTPNKL SEGLI
//
