ID A0A0F0LBC3_9MICO Unreviewed; 1159 AA.
AC A0A0F0LBC3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN Name=putA_2 {ECO:0000313|EMBL:KJL30423.1};
GN ORFNames=RS83_00809 {ECO:0000313|EMBL:KJL30423.1};
OS Microbacterium oxydans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=82380 {ECO:0000313|EMBL:KJL30423.1, ECO:0000313|Proteomes:UP000033640};
RN [1] {ECO:0000313|EMBL:KJL30423.1, ECO:0000313|Proteomes:UP000033640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BEL4b {ECO:0000313|EMBL:KJL30423.1,
RC ECO:0000313|Proteomes:UP000033640};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL30423.1}.
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DR EMBL; JYIW01000019; KJL30423.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0LBC3; -.
DR PATRIC; fig|82380.11.peg.836; -.
DR Proteomes; UP000033640; 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}.
FT DOMAIN 129..430
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 517..934
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 460..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 722
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 756
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1159 AA; 123469 MW; 2B6B70C7D250BB85 CRC64;
MTAVDTTPRT SEVAAVVQRW LTESETHPVE PAAQRLAEVL KDPRGLDFTV GFVDGVMRPE
DLSVAGRKLA EISEITPTLL PWVLRSAIKT GGFFAPKLPG VVVPISRRVL RAMVGHLVLD
ATPSKLGPAI AKLRKSGNRL NLNLLGEAVL GEREAGHRLQ GTRDFLARDD VDYVSIKVSS
VVSQLSMWSF DEAVADVVEK LTPLYELAAK AEAKGPSTGS GTQKFINLDM EEFRDLDLTI
AAFTAILDQP GLENLEAGIV LQAYLPDALG AMQHLQEWAA ARRAKGGAPI KVRVVKGANL
AMEHVDAAVH GWPLATYGTK QDSDTNYKRV LDWALTPERL DAVRIGVAGH NLFDIAYTWL
LSRARGVDGG SLVEYEMLLG MATGQAEAVR KDVGRLLLYT PVVNPAEFDV AIAYLVRRLE
ENASQENFMS AVFELASNPT LLTRERERFE RSLAALEADR SVPASNRVQD RTTEADAATP
TTAFHNQPDT DPALDANRAW GREILQRSVD STLGVDAIAA ARVETTEQLD GIFVAATAAA
AQWAARPAAE RAEILHRAGD ELAARRGQLI EIMAHEAGKT IAEADPEISE AIDFAHYYAE
RAKDLETVSG AAFIPSKVTV VTPPWNFPVA IPAGGVLAAL ASGSGVVIKP AKLTQRCGAV
MIEALWAAGV PRDLLALVDL ASRDLGTRLV SSPAVDRVIL TGAYETAQLF RSFRSDLPLL
GETSGKNAII VTPSADLDLA AADVARSAFG HAGQKCSAAS LAILVGSVAD SKRFQRQLVD
AVSSMRVGLP DDPATQMGPI IEPADGKLLA ALTELGAGES WLVKPKQLDD EGKQWTPGVK
TGVRAGSYFH MTEFFGPVLG IMVAKDLDEA IRLQNAVDYG LTAGIHSLDS TEVATWLDRV
EAGNLYVNRG ITGAIVQRQP FGGWKRSAVG AGAKAGGPNY LFGLGEWAPA ELPAVAPDAA
VTPAVDALLR AAAGELDAVE SEWLQRAAAS DERAWVDEFG AITDKSGLGV ERNLFRYRPV
AVDVRIAEGA PLVEGVRVLA AALRSGSPFT VSSSKLPSGI EKVLRAQGVS IAHEKDAAWA
KGFAKSVSKA AHSWARVRLV GGDASALFEA LGGLPDVAVW SHAVTGAGRV EILPFLHEQA
VSITNHRFGN PTGLTDGVI
//
