ID A0A0U2WPE8_9MICC Unreviewed; 1164 AA.
AC A0A0U2WPE8;
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=AS188_00540 {ECO:0000313|EMBL:ALU38484.1}, KFL01_18270
GN {ECO:0000313|EMBL:GEO92521.1};
OS Kocuria flava.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=446860 {ECO:0000313|EMBL:ALU38484.1, ECO:0000313|Proteomes:UP000057181};
RN [1] {ECO:0000313|EMBL:ALU38484.1, ECO:0000313|Proteomes:UP000057181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO-9041 {ECO:0000313|EMBL:ALU38484.1,
RC ECO:0000313|Proteomes:UP000057181};
RA Zhou M., Dai J.;
RT "Complete Genome Sequence of Kocuria flava strain HO-9041.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GEO92521.1, ECO:0000313|Proteomes:UP000321155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 107626 {ECO:0000313|EMBL:GEO92521.1,
RC ECO:0000313|Proteomes:UP000321155};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Kocuria flava NBRC 107626.";
RL Submitted (JUL-2019) 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}.
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DR EMBL; CP013254; ALU38484.1; -; Genomic_DNA.
DR EMBL; BJZR01000047; GEO92521.1; -; Genomic_DNA.
DR RefSeq; WP_058857198.1; NZ_CP013254.1.
DR AlphaFoldDB; A0A0U2WPE8; -.
DR STRING; 446860.AS188_00540; -.
DR KEGG; kfv:AS188_00540; -.
DR OrthoDB; 9812625at2; -.
DR Proteomes; UP000057181; Chromosome.
DR Proteomes; UP000321155; 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:UP000057181}.
FT DOMAIN 149..440
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 523..950
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 474..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 733
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 767
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1164 AA; 124082 MW; A3DC8A965742C96F CRC64;
MTTVPAPAAP VLHECPAPDP AAHAFLPEGL AEEAVALVRR WLAEAEQYPA DAAARHLAGV
LKDPHGLDFT VGFVDGVVRP EDDAVAARNL ARLAPRVPAF LPWYLRGAVR AGGALAPAAP
RLVVPAARRA LREMVGHLIV DADPRRLGRS IAAIRTEGVR LNLNLLGEAV LGTREADRRL
EGTRALLARP DVDYVSVKVS SVVGPHSPWA FDEAVAEVVD KLAPLYEQAA ASPEPKFVNL
DMEEYKDLDL TVAVFTRLLE QPRFKHLEAG IVLQAYLPDS LAAMIRLQEW AAARRAAGGA
PVKVRVVKGA NLPMERVEAS LHDWPLATWS TKQDSDTHYK RVLDYALRPE HTDAVRIGVA
GHNLFDVAFA WLLAGRRGVR GAVEFEMLLG MATGQAEAVR REVGSLLLYT PVVHAAEFDV
AIAYLVRRLE EGSSPENFMS AVFELAGNEH AFERERQRFL ASLAALDDTV PAPHRVQDRT
RPEPPVPAED FASTPDTDPA VAVNRAWGRE ILARVPGSRA GAATVAAARL RTEDELEEVV
TAALDAGRGW AGLSGAQRAA VLHRAGDALA ARRAELLEVA AAEAGKTLDQ SDPEVSEAID
FAHYYAERAR ELDDVDGARF VPSRLTVVTP PWNFPVAIPA GSALSALAAG SPVVFKPAGP
TRRCGAVVAE AIWEALDAAG IDRAVLSLVD LEERALGRQL IAHPAVERVV LTGAYETAEL
FRSFRPDLPL LAETSGKNAL VVTPSADLDL AAKDVAHSAF GHAGQKCSAA SLVVLVGSVA
RSRRFRDQLL DAVTSLTVDR ATNPAAQMGP LTEPASGKLL RALTTLEEGQ SWLVEPRRLD
DEGRLWTPGV RTGVRRGSEF HQVEYFGPVL GVMTAETLEE AVAIQNEVEY GLTAGLHSLD
PAEIGYWLEH VEAGNVYVNR GITGAIVRRQ PFGGWKKSAV GPGTKAGGPN YLTGLGGWVP
AAPRGTGGDL GDGPAAELLA AARRLLHAAE AERLEQALRL DAAAWAEEFG AARDVSQLYA
ERNVFRYLPV PVTVRHGGDV PVGELLRVLG AGLRAGSPLT VSTAEELPAP VAAVLAAHGA
DLRVEDEHAW SASAAAAGAG RVRLVGGDRA DLIAATGGRP DVAVYADPVT AAPRVELLPF
LREQAVSITA HRFGTPDHLT DGLI
//
