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Database: UniProt
Entry: A0A014M378_9GAMM
LinkDB: A0A014M378_9GAMM
Original site: A0A014M378_9GAMM 
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
//
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