ID A0A161SVE7_9MICO Unreviewed; 1144 AA.
AC A0A161SVE7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN ORFNames=AVW09_00580 {ECO:0000313|EMBL:KZE43273.1};
OS Microbacterium sp. T32.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1776083 {ECO:0000313|EMBL:KZE43273.1, ECO:0000313|Proteomes:UP000076494};
RN [1] {ECO:0000313|Proteomes:UP000076494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T32 {ECO:0000313|Proteomes:UP000076494};
RA Hong K.W.;
RT "Whole genome sequencing of Bhargavaea cecembensis T14.";
RL Submitted (JAN-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:KZE43273.1}.
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DR EMBL; LQQP01000001; KZE43273.1; -; Genomic_DNA.
DR RefSeq; WP_063256133.1; NZ_LQQP01000001.1.
DR AlphaFoldDB; A0A161SVE7; -.
DR STRING; 1776083.AVW09_00580; -.
DR OrthoDB; 9812625at2; -.
DR Proteomes; UP000076494; 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:UP000076494}.
FT DOMAIN 143..426
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 509..932
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 456..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 715
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 749
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1144 AA; 121894 MW; 77FCBC2B2849F300 CRC64;
MSLTDVTRSE VAPADLADEA VALVRRWLAE SRDEPVDAAA TRLAGVLRDP NGLAFTVGFV
DGVVRPEDLR VAAANLAGLA PLVPGFLPLH LKAAIRLGAL TAPLLPRVVV PAARAALRSM
VRHLIVDASD RRLGDAIAAI RGRGEGIRLN VNLLGEAILG KKEAARRLEG TRRLLARDDV
DYVSIKVSST VAPHTPWAFD AAVADAVSAL RPLYRVAKET GTFLNLDMEE FKDLDLTLAV
FETLLGEPEF HGVEAGIVLQ AYLPDALAAM IRLQEWTAAR VASGGAPIKV RVVKGANLPM
ERVDADVHDW PLATWPSKQA TDASYKAVLD YALRPEHTAH VRIGVAGHNL FDVALAWLLA
ERRGVTGGID VEMLLGMATA QQAVVRRTVG SILLYTPVVH PQEFDVAIAY LIRRLEEGAS
SENFMSAVFD LGTHEALFAR ERDRFLASLA DMPTGVPASH RVQDRTAAPE PAPRDGFRNT
PDSDPAIAAN RAWAGRIVTR MATSRLGADT IAAHTVTDES VLDERIRAAA AAAVAWRELG
ADARAEILHR AGDALEARRA ELIEVMGAEC GKVVEQSDPE VSEAIDFAHY YAEQGGRLER
VDGARFTPAG LTVVTPPWNF PVAIPAGSTL AALAAGSAVV IKPAALAERS GAVMVEALWE
AGIPRDVLTL VQVSENDLGR QLLTHPAVDR VVLTGAYETA ELFRSFRPDL PLLAETSGKN
AVIVTPSADL DLAAKDVALS AFGHAGQKCS AASLVVLVGS VATSRRFRDQ LVDAVESLEV
GMPWDDAARV GPLIEPAQGK LLRALTTLEP GQRWVVEPRR LDEDGRLWRP GIREGVQPGS
EFHRTEYFGP VLGIMTAETL DEAIDIVNAI EYGLTSGLHA LDETEIQRWL ARIEAGNAYV
NRGTTGAIVQ RQPFGGWKKS AVGAGTKAGG PHYLFGFGSW TDAEASAPRL ADALAGPACA
AVPAADREWL ASALASDAAV WASEFSVARD VTGLESEQNV LRYGAVPVTV RLEDAADVAL
VRVVAAGVRA GSAVTVSAGR ELTPAVRAWL EGAGVAYDIE DAAAWARRAA RLARTGGRVR
LLGGSVERFA ADTAGSPAVA LYAGDPTRAG EVEMLPFLRE QAVSITAHRF GTPRRYVVPS
LVRA
//
