ID A0A014M378_9GAMM Unreviewed; 1199 AA.
AC A0A014M378;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
DE Flags: Fragment;
GN ORFNames=BG55_06790 {ECO:0000313|EMBL:EXU76286.1};
OS Erwinia mallotivora.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU76286.1, ECO:0000313|Proteomes:UP000019918};
RN [1] {ECO:0000313|EMBL:EXU76286.1, ECO:0000313|Proteomes:UP000019918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU76286.1,
RC ECO:0000313|Proteomes:UP000019918};
RA Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L.,
RA Mat Amin N.;
RT "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback
RT pathogen.";
RL Submitted (FEB-2014) 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:EXU76286.1}.
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DR EMBL; JFHN01000034; EXU76286.1; -; Genomic_DNA.
DR RefSeq; WP_034935645.1; NZ_JFHN01000034.1.
DR AlphaFoldDB; A0A014M378; -.
DR STRING; 69222.BG55_06790; -.
DR PATRIC; fig|69222.5.peg.1399; -.
DR OrthoDB; 9812625at2; -.
DR Proteomes; UP000019918; 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:0006561; P:proline biosynthetic process; IEA:InterPro.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:InterPro.
DR CDD; cd07125; ALDH_PutA-P5CDH; 1.
DR Gene3D; 3.20.20.220; -; 1.
DR Gene3D; 1.20.5.460; Single helix bin; 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; IPR024089; PRODH_PutA_dom_I/II.
DR InterPro; IPR024082; PRODH_PutA_dom_II.
DR InterPro; IPR002872; Proline_DH_dom.
DR InterPro; IPR005933; PutA_C.
DR NCBIfam; TIGR01238; D1pyr5carbox3; 1.
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 Pfam; PF14850; Pro_dh-DNA_bdg; 1.
DR PIRSF; PIRSF000197; Bifunct_PutA; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
DR SUPFAM; SSF81935; N-terminal domain of bifunctional PutA protein; 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:UP000019918}.
FT DOMAIN 28..140
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 149..450
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 540..986
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 764
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 798
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EXU76286.1"
SQ SEQUENCE 1199 AA; 130107 MW; 5369103E5750393E CRC64;
PSQQTYRLAH QLADTLRHQK GAGGRAGMVQ NLLQEFSLSS QEGVALMCLA EALLRIPDKP
TRDALIRDKI SNGNWQSHLG RSRSLFVNAA TWGLLFTGRL VATHNEANLS HSLNRIIGRR
GEPLIRKGVD MAMRLMGEQF VTGETIAEAL ANARKLEEKG FRYSYDMLGE AALTARDAEA
YLLSYQQAIH AIGKASNGRG IYEGPGISIK LSALHPRYSR GQYERVMNEL WPVLKSLTLL
ARSYDIGINI DAEEADRLEL SLDLLEKLCF EPELEGWNGI GFVIQAYQKR CPLVIDALTD
LAGRSQRRLM VRLVKGAYWD SEIKRAQQEG LEGYPVFTRK VYTDISYLAC ARKLLAVPNL
IYPQFATHNA HTLAAIYQLA GNNYYPGQYE FQCLHGMGEP LYEQVVGKVA DGKLNRPCRI
YAPVGTHETL LAYLVRRLLE NGANTSFVNR IADTSLAVED LVACPVDEVE KLARSEGAIG
LPHPRIPLPR DIYGAQRQNA AGLDLANEHR LASLSSALLN SAIQPWQVAP LIDGVTSPGD
ALPVINPAEP TDVVGYVRHA STADVDTALD AAVNAAPIWF ATPAQERAAI LHRAAGLMEN
QLQHLLGVLV REAGKTFSNA IAEVREAVDF LHYYAAQVSD DFDNETHRPL GPVVCISPWN
FPLAIFTGQV AAALSAGNCV LAKPAEQTPL IAALAVQLLY DAGVPRGALQ LLPGEGETVG
ARLTADSRVR GVMFTGSTAV ASLLQRTLAS RLDPQGRPVP LIAETGGLNA MIVDSSALTE
QVVIDILASA FDSAGQRCSA LRLLCIQDDV AEHTLKMLRG AMSECRMGNP ERLSTDIGPV
IDKEAKQAIE QHIAAMRSKG MSVYQAALNC DQDCKEWQSG TFVQPTLIEL QSVSDLDKEV
FGPVLHVVRY SRNTLPQLVE QINAQGYGLT MGIHTRIDET IGQVSQRAHV GNLYVNRNMV
GALVGVQPFG GEGLSGTGPK AGGPLYLYRL LSSRPDDALR ITLERQDALL PADTTLRATL
LGAHQALTAW AEEKPHLAAI CTRFAALAQS GTVRLLAGPT GERNSYTLLP RERVLALADN
EQDALVQLAA ITATGSRALW QDDELHRTLC SALPDEVRAR IDFASAPLQQ HFDAVIFHGD
ADQLGEVCQQ VAAREGAIVS VQGFDRGDTG LLLERLLIER AISVNTAAAG GNASLMTIG
//